1pvh
From Proteopedia
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Crystal structure of leukemia inhibitory factor in complex with gp130
Contents |
Overview
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.
Disease
Known disease associated with this structure: Stuve-Wiedemann syndrome/Schwartz-Jampel type 2 syndrome OMIM:[151443]
About this Structure
1PVH is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130., Boulanger MJ, Bankovich AJ, Kortemme T, Baker D, Garcia KC, Mol Cell. 2003 Sep;12(3):577-89. PMID:14527405
Page seeded by OCA on Thu Feb 21 14:32:59 2008
