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COPS5 binds COPS6. 69 / 96
23 3 | 25 44
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"Therefore, to characterise further this complex, we probed the association of CSN5 ΔC and CSN6 ΔC by NMR to help define the regions responsible for the interaction."
25144743
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"It is noteworthy that, although the interaction between CSN5 ΔC and CSN6 ΔC was impaired by the H44A or to a stronger extent by the V115A substitution, the effect of these variants remains modest (2 to 5-fold)."
25144743
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"However, the Y2H results showed that Csn5 only directly interacted with Csn6 but not the other five Csn subunits ( xref ), implying that Csn5 may associate but not directly interact with others."
37168110
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"Exploiting the above detailed finding that CSN5 ΔC and Nedd8 interaction proceeds through similar surfaces to that of AMSH-LP-distal ubiquitin's ( xref , xref ), a complex composed of CSN5 ΔC displaying an AMSH-LP-like Ins-1 conformation and of Nedd8 was assembled and used to probe the association of CSN5 ΔC and CSN6 ΔC ."
25144743
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"As shown in xref , Flag-Csn6 fusion proteins could be identified in proteins copurified with GFP-Csn5, further confirming the interaction between Csn5 and Csn6."
37168110
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"Each of the above multiprotein complexes contains a single heterodimer of MPN proteins, usually with one catalytically active and one inactive monomer (POH1-Rpn8 in the proteasome, CSN5-CSN6 in the signalosome and BRCC36-Abraxas in the RAP80 complex)."
35501388
sparser
"This analysis could strengthen the view that CSN5 ΔC and CSN6 ΔC interact through an architecture reminiscent of the Rpn11 ΔC /Rpn8 ΔC complex."
25144743
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"Both complexes contain an MPN dimer (CSN5-CSN6 in the COP9 signalosome and POH1-Rpn8 in the proteasome lid) and six PCI-domain proteins."
35501388
sparser
"In addition to the Csn5-Csn6 interaction, nine other interaction pairs were detected in this study, including Csn1-Csn2, Csn1-Csn3, Csn1-Csn4, Csn2-Csn3, Csn3-Csn4, Csn3-Csn6, Csn4-Csn6, Csn4-Csn7, and Csn6-Csn7 ( xref )."
37168110
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"We can conclude that CSN6 51–187 dimeric interactions may provide the basis for CSN5 homodimer or CSN5-CSN6 heterodimer [28–30] ."
22575649
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"Several interactions, including Csn1-Csn2, Csn1-Csn4, Csn4-Csn7, Csn4-Csn6, and Csn5-Csn6, were all demonstrated in these organisms ( xref ; xref )."
37168110
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"Another CSN-associated DUB is the signal transducing adapter molecule (STAM) binding protein like 1 (STAMBPL1), which is a ubiquitous metalloprotease DUB that copurifies with the CSN and interacts wit[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
36041947
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"CSN5 and CSN6, which have an MPN (Mpr1 and Pad1 N-terminal) domain, form a dimer and are embedded at the core of the helical bundle."
29616013
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"The structure reaffirms the conserved activation mechanism of the deneddylation machinery, including conformational clamping of CRL2 by CSN2/CSN4, release of the catalytic CSN5/CSN6 heterodimer, and s[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
33271439
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"The above suggests that the MPN dimer (CSN5–CSN6 dimer) could be highly conserved."
33806190
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"Molecular dynamics simulation studies further suggest that heterodimerization of CSN5 with CSN6 facilitates inhibitor binding by stabilizing an open ins-1 loop conformation [ 58 ]."
36041947
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"Structurally, CSN6 and CSN5 form a heterodimer through MPN domain and the dimer is topologically knotted to engage in Cullin deneddylation xref ."
25395170
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"MD simulations studies and binding energy analysis revealed that the selective binding of the inhibitors can be only explained by the consideration of larger heterodimeric complexes of Rpn11 (Rpn8-Rpn11) and CSN5 (CSN5-CSN6)."
30356695
sparser
"In the crystal structure of CSN5-CSN6 heterodimer, initial Ins-1 loop (98–109) conformation blocks the distal ubiquitin binding site which we also observed in cryo-EM structure of Rpn11."
30356695
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"Rpn8-RPN11 and CSN5-CSN6 heterodimeric states are shown in Figure xref ."
30356695
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"Binding of capzimin and CSN5i-3 to monomeric CSN5 and CSN5-CSN6 heterodimer."
30356695
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"MD simulation of capzimin with monomeric CSN5 and CSN5-CSN6 heterodimer revealed that its binding to CSN5 is also influenced by the CSN6 (Figure xref )."
30356695
sparser
"In the CSN5-CSN6 heterodimer we observed that CSN5i-3 is stable (Figure xref ) and its conformation is very close to the conformation reported in the crystal structure (Figure xref )."
30356695
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"However, in the CSN5-CSN6 heterodimer, CSN5i-3 forms stable H-bonds with both Thr154 and Asn158 (Figure xref and Figure xref )."
30356695
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"For example, the main interactions at the interface in Rpn11-Rpn8 [24] and CSN5-CSN6 [25] heterodimers involve the residues from the two helices, and the α2-helix in AMSH-LP plays a role in substrate [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
27240952
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"This may be the reason behind lower flexibility of Ins-1 loop in the monomeric CSN5 compared to the CSN6 bound CSN5."
30356695
sparser
"However, in the CSN5-CSN6 heterodimer, capzimin displayed a monodentate coordination with Zn 2+ and only low occupancy H-bonds with side chains of Met78, Arg106, and Asn158 (Figure xref )."
30356695
sparser
"Since the N-terminal region of ODR4 is predicted to have an MPN domain, it is tempting to suggest that the interactions seen between the MPN domains in the Rpn11-Rpn8 [24] and CSN5-CSN6 [25] multi-pro[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
27240952
sparser
"Considering the Rpn8-Rpn11 and CSN5-CSN6 heterodimers, we found that residues in the distal ubiquitin site are responsible for selectivity and must be taken into consideration for the design of selective inhibitors of CSN5 and Rpn11 in future studies."
30356695
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"Alternatively, based on recent finding on the structure of eight-unit COP9 complex XREF_BIBR, it is possible to modulate COPS5 activity by tackling the interactions between COP9 subunits, particularly the interaction between COPS5 and COPS6 and CSN6 subunits that is crucial for maintaining the isopeptidase activity."
27375289
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"The cap sits at the top of the box and consists of a CSN5–CSN6 heterodimer ( xref ) ( xref )."
28271482
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"Taken together, COPS5 and COPS6 were associated with the survival of the HNSCC cells and could be detected in tumor samples using IHC."
34630710
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"Structural data provide evidence for coordinated domain changes of CSN2, CSN4, and CSN7 and the CSN5-CSN6 heterodimer induced by neddylated CRL4A converting CSN5 into its active conformation [37]."
32708147
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"In analogy to the CSN5-CSN6 heterodimer, RPN11 partners with another MPN domain protein, RPN8, possessing an inactive JAMM domain."
32708147
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"Sitting atop…is the CSN5–CSN6 tomato….” [ xref ])."
31195722
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"Interaction of the complex with a NEDDylated CRL leads to a series of conformational change events in Csn2, Csn4 and Csn7, triggering rearrangements in the Csn5–Csn6 dimer, resulting in Csn5 activation by priming the Csn5 JAMM/MPN + motif for deNEDDylation [ xref , xref ]."
33099217
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"The MPN domains of the CSN5 and CSN6 heterodimer rest on the helical bundle while their carboxy terminal helical tails are inserted into the helical bundle."
26437438
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"Structural and Biochemical Characterization of the Cop9 Signalosome CSN5 and CSN6 Heterodimer."
25144743
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"The structure of the CSN5-CSN6 heterodimer (Figure S3A) was extracted from the crystal structure of human COP9 signalasome (PDB_code: 4D10) (Lingaraju et al., 2014) C-terminal regions of CSN5 (258–333) and CSN6 (215–316) were also deleted since they are not involved in catalysis and heterodimer formation can take place without them."
30356695
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"The processed CSN5-CSN6 heterodimer is shown in Figure 3B and Figure S3C."
30356695
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"Structural data provide evidence for coordinated domain changes of CSN2, CSN4, and CSN7 and the CSN5-CSN6 heterodimer induced by neddylated CRL4A converting CSN5 into its active conformation [ xref ]."
32708147
reach
"In the crystal structure of CSN5-CSN6 heterodimer, initial Ins-1 loop (98–109) conformation blocks the distal ubiquitin binding site which we also observed in cryo-EM structure of Rpn11."
30356695
sparser
"In analogy to the CSN5-CSN6 heterodimer, RPN11 partners with another MPN domain protein, RPN8, possessing an inactive JAMM domain."
32708147
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"These data suggests a hierarchy in the catalytic activity over the enzymatic system and the substrate type, with the inactive CSN5 DeltaC, WT form, CSN5 DeltaC, R106T that has basal activity, the MPN heterodimer alone that has robust isopeptidase activity on non physiological substrates and the CSN5 and CSN6 heterodimer in the context of CSN that recapitulates strong activity on both non physiological and physiological substrates."
25144743
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"Binding of capzimin and CSN5i-3 to monomeric CSN5 and CSN5-CSN6 heterodimer."
30356695
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"First, the catalytic activity efficiency can be achieved by an increase of affinity for Nedd8 observed either in the CSN5 and CSN6 complex or by the conformational relaxation of the Ins-1 segment."
25144743
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"MD simulation of capzimin with monomeric CSN5 and CSN5-CSN6 heterodimer revealed that its binding to CSN5 is also influenced by the CSN6 (Figure 10)."
30356695
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"The catalytic subunit CSN5 forms a subcomplex with CSN6 and CNS4."
26073511
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"In the CSN5-CSN6 heterodimer we observed that CSN5i-3 is stable (Figure 12C) and its conformation is very close to the conformation reported in the crystal structure (Figure S6)."
30356695
reach
"However, in the CSN5-CSN6 heterodimer, CSN5i-3 forms stable H-bonds with both Thr154 and Asn158 (Figure S5D and Figure 13B)."
30356695
reach
"As shown in Figure 2C, Flag-Csn6 fusion proteins could be identified in proteins copurified with GFP-Csn5, further confirming the interaction between Csn5 and Csn6."
37168110
reach
"This may be the reason behind lower flexibility of Ins-1 loop in the monomeric CSN5 compared to the CSN6 bound CSN5."
30356695
reach
"However, in the CSN5-CSN6 heterodimer, capzimin displayed a monodentate coordination with Zn and only low occupancy H-bonds with side chains of Met78, Arg106, and Asn158 (Figure S5B)."
30356695
sparser
"The MPN domains of CSN5 and CSN6 form a stable heterodimer."
25144743
sparser
"Previous structural studies of the CSN suggested that CSN5 and CSN6 interact xref , xref ."
25144743
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"The association of the 1–257 and 31–211 domains of CSN5 and CSN6, amenable to soluble bacterial expression, referred to as CSN5 ΔC and CSN6 Δ , respectively ( xref , xref ) was probed by ITC experiments."
25144743
sparser
"For instance, in plant cells, isoforms have been identified for the MPN‐domain subunits CSN5 (CSN5A and CSN5B) and CSN6 (CSN6A and CSN6B) which form four distinct CSN variants."
27833851
sparser
"As a result, the CSN5-CSN6 dimer undergoes conformational rearrangement to facilitate movement toward the directed CRL4A DDB2 [ xref ]."
35883466
sparser
"Then, with the binding of neddylated SCF Skp2/Cks1 , topological conformation change occurs in the CSN5-CSN6 dimer, resulting in CSN5 activation."
35883466
sparser
"Structurally, CSN6 and CSN5 form a heterodimer through MPN domain, and the dimer is topologically knotted to engage in Cullin deneddylation ( xref )."
26267535
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"We can conclude that CSN6 51–187 dimeric interactions may provide the basis for CSN5 homodimer or CSN5-CSN6 heterodimer [28–30] ."
22575649
sparser
"While in the absence of the substrate (neddylated cullin) CSN5 is in an inactive conformation, substrate binding leads to a dramatic domain motion of CSN4, which moves the CSN5–CSN6 dimer away from th[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26096786
sparser
"The helical bundle closely associated with the CSN5–CSN6 dimer [17] is perhaps involved in conformational changes regulating CSN activity in response to phosphorylation."
26096786
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"In our CSN6 homodimer structure, alpha1 and alpha2 from one monomer interact with alpha2 and alpha1 from another monomer, respectively, while in the CSN5 and CSN6 heterodimer, alpha1 and alpha2 helice[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
25242525
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"Moreover, in the CSN5 and CSN6 heterodimer, alpha4 helix of CSN6, a C-terminal extension of the MPN domain, interacts with alpha6 helix of CSN5."
25242525
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"Unlike the N-terminal, the extended C-terminal helix of each CSN1–CSN8 subunit forms a helical bundle while the CSN5 and CSN6 heterodimers with MPN domains adopt globular conformations just above the helical bundle [ xref , xref ]."
35883466
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"The catalytic subunit CSN5 forms a subcomplex with CSN6 and CNS4."
26073511
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"In the presence of CRL4A, conformational changes in CSN2, CSN4, and CSN7 affect the CSN5-CSN6 dimer and activate CSN5."
39600336
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"38 Also the MPN domain is involved in heterodimerization between CSN6 and CSN5 to regulate Cullin neddylation."
33101846