Sandbox Reserved 830: Difference between revisions
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The AB loop is composed of two α-helices from Pro43 to Arg46 and Glu59 to Gly64, while the residues in between pack closely and extensively against helix D. Comparatively, BC and CD loops are less stacking to the core. The BC loop located on the top of the four-helix bundle exhibits an important amount of B factors, along with several more classical secondary structures, which are a 310 helix between residues Ala95 and Asp97 followed by the α helix up to Ser101. | The AB loop is composed of two α-helices from Pro43 to Arg46 and Glu59 to Gly64, while the residues in between pack closely and extensively against helix D. Comparatively, BC and CD loops are less stacking to the core. The BC loop located on the top of the four-helix bundle exhibits an important amount of B factors, along with several more classical secondary structures, which are a 310 helix between residues Ala95 and Asp97 followed by the α helix up to Ser101. | ||
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Site 2 of OSM binds to gp130 subunit with four residues located in helices A and C. The most important residues are Asn124 and Gly120 which are situated in helix C. Two other residues contribute to binding the linking: Gln16 and Gln20, located in helix A. OSMR allows binding of OSM on three residues: Tyr196, Phe169 and Glu282. | Site 2 of OSM binds to gp130 subunit with four residues located in helices A and C. The most important residues are Asn124 and Gly120 which are situated in helix C. Two other residues contribute to binding the linking: Gln16 and Gln20, located in helix A. OSMR allows binding of OSM on three residues: Tyr196, Phe169 and Glu282. | ||
Site 3 of OSM binds to LIFR or OSMR thanks to two residues: Phe160 and Lys163, located in the N-terminal end of helix D. These amino acids are conserved in all cytokines. | Site 3 of OSM binds to LIFR or OSMR thanks to two residues: Phe160 and Lys163, located in the N-terminal end of helix D. These amino acids are conserved in all cytokines. | ||
[[Image:Osm interact osmr.png|frame|left|Complementarity between the interaction surfaces of hOSM and gp130.The solvent-accessible surfaces of site 2 on hOSM (left) and the cognate binding site on gp130 (right) are displayed with areas contributed by residues implicated in binding highlighted as coloured patches.]] [[Image:Oncostatin site3.jpg|frame|center| Site 3 configuration with residues for OSMR and LIFR binding in red.]] | [[Image:Osm interact osmr.png|frame|left|Complementarity between the interaction surfaces of hOSM and gp130.The solvent-accessible surfaces of site 2 on hOSM (left) and the cognate binding site on gp130 (right) are displayed with areas contributed by residues implicated in binding highlighted as coloured patches.]] [[Image:Oncostatin site3.jpg|frame|center| Site 3 configuration with residues for OSMR and LIFR binding in red.]] | ||