1pvh
From Proteopedia
(New page: 200px<br /> <applet load="1pvh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pvh, resolution 2.50Å" /> '''Crystal structure o...) |
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| - | [[Image:1pvh.gif|left|200px]]<br /> | + | [[Image:1pvh.gif|left|200px]]<br /><applet load="1pvh" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1pvh" size=" | + | |
caption="1pvh, resolution 2.50Å" /> | caption="1pvh, resolution 2.50Å" /> | ||
'''Crystal structure of leukemia inhibitory factor in complex with gp130'''<br /> | '''Crystal structure of leukemia inhibitory factor in complex with gp130'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Gp130 is a shared cell-surface signaling receptor for at least ten | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PVH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with IOD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PVH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=IOD:'>IOD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PVH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Baker, D.]] | [[Category: Baker, D.]] | ||
| - | [[Category: Bankovich, A | + | [[Category: Bankovich, A J.]] |
| - | [[Category: Boulanger, M | + | [[Category: Boulanger, M J.]] |
| - | [[Category: Garcia, K | + | [[Category: Garcia, K C.]] |
[[Category: Kortemme, T.]] | [[Category: Kortemme, T.]] | ||
[[Category: IOD]] | [[Category: IOD]] | ||
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[[Category: signaling]] | [[Category: signaling]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:59 2008'' |
Revision as of 12:33, 21 February 2008
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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
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