IndraLab

Statements

Capsid protein binds CALM1. 13 / 13
| 13
sparser
"Experimentally, capsid disruption in the presence of CAM-As proceeds over hours to days even at high small-molecule concentrations, [ xref ] consistent with the metastable character of CAM-bound capsids observed here on the microsecond timescale."
41040136
sparser
"All-atom models of intact, CAM-bound HBV Cp149 capsids were prepared based on crystal structures of pre-formed capsids complexed with AT130 (PDB 4G93, 4.2 Å), [ xref ] HAP1 (PDB 2G34, 5.0 Å), [ xref ] and HAP18 (PDB 5D7Y, 3.9 Å). [ xref ] The AT130- and HAP18-bound capsid models contain CAMs in all B and C sites and are referred to as saturated."
41040136
sparser
"The results showed that in HepAD38 and HepG2-HBV1.3 cells, only C-39 and the known type I CAM BAY 41-4109 dramatically inhibited capsid formation, while ETV and the other eight compounds showed much less or no inhibition effects ( xref C)."
35215939
sparser
"MD results suggest that the first CAM molecule is most likely to bind the intact capsid in a B site, and that B site occupancy can increase the accessibility of adjacent C sites, indicating potential positive cooperativity during CAM uptake."
41040136
sparser
"Figure  xref shows the residue-specific chemical-shift differences between the apo and CAM-bound capsids for the different compounds plotted on the Cp dimer 3D structure (PDB 5d7y xref ) (for chemical-shift perturbations (CSPs) see Supplementary Fig.  xref )."
36709212
sparser
"These are not only academic questions as they also relate to the interpretation of capsid-CAM interactions in vivo."
| PMC
sparser
"The CAM (-N), leading to the formation of morphologically normal capsids and the CAM (-A), leading to aberrant HBV capsid structures."
34918017
sparser
"Interestingly,dimer pair dynamics in the HAP1-bound case are more similar to the AT130-bound than any other system, despite the fact that these represent the most and least faceted CAM-bound capsids, respectively."
41040136
sparser
"Interestingly, CAM binding of assembled capsids induces significant structural changes in the HAP pocket and triggers overall and global structural alterations in Cp dimer, tetramer and capsids."
40143261
sparser
"Compared to a cryo-EM analysis of CAM-bound capsids that mostly revealed that CAM induced Cp tertiary and quaternary structural changes, the crystallography of CpY132A heximers revealed a more detailed interaction of the CAM molecule with amino acid residues of Cp at the HAP pocket due to an improved resolution [ xref , xref ]."
40143261
sparser
"Notably, experimental structures of CAM-bound capsids have been obtained using the Cp150 construct, a truncation mutant comprising the assembly domain with a C-terminal cysteine substitution at position 150. [ xref ] The engineered cysteine promotes disulfide cross-links between neighboring dimers, stabilizing the shell and protecting it from CAM-induced dissociation."
41040136
sparser
"In our initial efforts to achieve this goal, we compared three computational chemistry methods for their ability to predict a panel of 35 naturally occurring Cp mutations that may confer resistance to representative CAM-A and CAM-E compounds with all the crystal or CryoEM structures of CAM-bound HBV capsids or CpY132 hexamers available in the protein database."
40143261
sparser
"A model of the quasi-equivalent sites from a capsid-CAM complex xref with a cysteine and maleimide modeled xref at position 124 in the capping helix emphasizes this difference ( xref )."
36651799