Sandbox Reserved 830: Difference between revisions
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OSM contains two binding sites for the heterodimer receptor: site 2 and site 3. | OSM contains two binding sites for the heterodimer receptor: site 2 and site 3. | ||
Site 2 of OSM binds to gp130 subunit with four residues located in helices A and C. The most important residues are <scene name='56/568028/Residues_binding_to_gp130/1'>Asn124 and Gly120</scene> which are situated in helix C. Two other residues contribute to the linking: <scene name='56/568028/Residues_binding_to_gp130/1'>Gln16 and Gln20</scene>, located in helix A. OSMR allows binding of OSM on three residues: Tyr196, Phe169 and Glu282 (Fig.2). | Site 2 of OSM binds to gp130 subunit with four residues located in helices A and C. The most important residues are <scene name='56/568028/Residues_binding_to_gp130/1'>Asn124 and Gly120</scene> which are situated in helix C. Two other residues contribute to the linking: <scene name='56/568028/Residues_binding_to_gp130/1'>Gln16 and Gln20</scene>, located in helix A. OSMR allows binding of OSM on three residues: Tyr196, Phe169 and Glu282 (Fig.2). | ||
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 (Fig.3). These amino acids are conserved in all cytokines<ref group=""> PMID: 10997905 </ref>. | Site 3 of OSM binds to LIFR or OSMR thanks to two residues: <scene name='56/568028/Site3_oncostatin/1'>Phe160 and Lys163</scene>, located in the N-terminal end of helix D (Fig.3). These amino acids are conserved in all cytokines<ref group=""> PMID: 10997905 </ref>. | ||