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| {{STRUCTURE_1pvh| PDB=1pvh | SCENE= }} | | {{STRUCTURE_1pvh| PDB=1pvh | SCENE= }} |
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| '''Crystal structure of leukemia inhibitory factor in complex with gp130'''
| | ===Crystal structure of leukemia inhibitory factor in complex with gp130=== |
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| ==Overview==
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| Gp130 is a shared cell-surface signaling receptor for at least ten different hematopoietic cytokines, but the basis of its degenerate recognition properties is unknown. We have determined the crystal structure of human leukemia inhibitory factor (LIF) bound to the cytokine binding region (CHR) of gp130 at 2.5 A resolution. Strikingly, we find that the shared binding site on gp130 has an entirely rigid core, while the LIF binding interface diverges sharply in structure and chemistry from that of other gp130 ligands. Dissection of the LIF-gp130 interface, along with comparative studies of other gp130 cytokines, reveal that gp130 has evolved a "thermodynamic plasticity" that is relatively insensitive to ligand structure, to enable crossreactivity. These observations reveal a novel and alternative mechanism for degenerate recognition from that of structural plasticity.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14527405}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14527405 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14527405}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Receptor]] | | [[Category: Receptor]] |
| [[Category: Signaling]] | | [[Category: Signaling]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:31:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:10:01 2008'' |