Sandbox Reserved 830: Difference between revisions

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Revision as of 13:01, 9 January 2014 view source Pierre-Yves Mocaer (talk \| contribs) 210 edits No edit summary ← Older edit		Revision as of 13:02, 9 January 2014 view source Pierre-Yves Mocaer (talk \| contribs) 210 edits No edit summary Newer edit →
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	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 ~~onfiguration~~ 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.]]