IndraLab

Statements

TSPO binds FN1. 14 / 14
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"Obviously, the intermolecular interaction between the PBR and FN1 should be an electrostatic interaction."
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"Comparing with an intermolecular polySia–PSTD interaction, the PBR–FN1 one is a relatively strong interaction."
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"The above three interactions (polySia–PSTD, FN1–PBR and PSTD–PBR interactions), may participate cooperatively in the NCAM polysialylation process [ xref , xref ]."
36499451
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"In order to initiate NCAM polysialylation, CMP-Sia, which is transported into the lumen of the Golgi complex, is fist bound to the PSTD in ST8Sia IV to generate polySia; then, formed polySia chains are released from the PSTD due to its configuration change when the PBR is bound to FN1 in NCAM; and finally, two connected cells are separated, and cell migration occurs due to the repulsive effect of the negative-charged anions between polySia chains located in the NCAM [ xref ]."
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"However, an isogenic strain producing OspC from B. garinii strain PBr, which binds fibronectin but not dermatan sulfate, colonized the skin, heart and bladder, but not joints."
32413091
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"As shown in xref , you can imagine that the PBR’s conformation should be changed when the PBR is bound to FN1, inducing a conformational change of the PSTD resulting in the polySia’s release from the bound PSTD, and finally resulting in the free polySia being bound to NCAM."
36499451
reach
"Obviously, the intermolecular interaction between the PBR and FN1 should be an electrostatic interaction."
36499451
reach
"In order to initiate NCAM polysialylation, CMP-Sia, which is transported into the lumen of the Golgi complex, is fist bound to the PSTD in ST8Sia IV to generate polySia; then, formed polySia chains are released from the PSTD due to its configuration change when the PBR is bound to FN1 in NCAM; and finally, two connected cells are separated, and cell migration occurs due to the repulsive effect of the negative-charged anions between polySia chains located in the NCAM [18]."
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"As shown in Figure 4, you can imagine that the PBR’s conformation should be changed when the PBR is bound to FN1, inducing a conformational change of the PSTD resulting in the polySia’s release from the bound PSTD, and finally resulting in the free polySia being bound to NCAM."
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"The Graphical Analysis of the PBR–FN1 Interaction."
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"In order to display a significant interaction between the PBR and FN1, the positions of R93, R82 and K83 should be closed to FN1 molecule in the space, and they are all exposed on the surface of ST8Sia IV model and are located in same side of the surface model of ST8Sia IV ( xref c)."
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"However, our attempts to fit the ITC data to a two binding site model to account for alternative and/or dual binding sites generated errors that were significantly larger than those generated when we fit the ITC data to a one-site model, supporting our interpretation of the interaction between PBR and FN1."
28233978
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"Incorporating the PBR wenxiang diagram into the molecular modeling of ST8sia IV may intuitively explain why R82, K83 and R93 are key amino acids for the PBR–FN1 interaction, and it also supports the previous findings using NMR spectroscopy [ xref ]."
36499451
sparser
"The three crucial amino acids, R82, K83 and R93, in the PBR are verified for the PBR–FN1 interaction by the relative positions of the wenxiang diagram of the PBR and FN1 in xref . xref is actually a combination of xref a,c."
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