1pvh
From Proteopedia
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|PDB= 1pvh |SIZE=350|CAPTION= <scene name='initialview01'>1pvh</scene>, resolution 2.50Å | |PDB= 1pvh |SIZE=350|CAPTION= <scene name='initialview01'>1pvh</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=IOD:IODIDE ION'>IOD</scene> | + | |LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= IL6ST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), LIF OR HILDA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= IL6ST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), LIF OR HILDA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pvh OCA], [http://www.ebi.ac.uk/pdbsum/1pvh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pvh RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Stuve-Wiedemann syndrome/Schwartz-Jampel type 2 syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=151443 151443]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Garcia, K C.]] | [[Category: Garcia, K C.]] | ||
[[Category: Kortemme, T.]] | [[Category: Kortemme, T.]] | ||
| - | [[Category: IOD]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
[[Category: cytokine]] | [[Category: cytokine]] | ||
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[[Category: signaling]] | [[Category: signaling]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:05:07 2008'' |
Revision as of 20:05, 30 March 2008
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| , resolution 2.50Å | |||||||
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| Ligands: | |||||||
| Gene: | IL6ST (Homo sapiens), LIF OR HILDA (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of leukemia inhibitory factor in complex with gp130
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.
About this Structure
1PVH is a Protein complex structure of sequences from Homo sapiens. 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 Sun Mar 30 23:05:07 2008
