1obx
From Proteopedia
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|PDB= 1obx |SIZE=350|CAPTION= <scene name='initialview01'>1obx</scene>, resolution 1.35Å | |PDB= 1obx |SIZE=350|CAPTION= <scene name='initialview01'>1obx</scene>, resolution 1.35Å | ||
|SITE= <scene name='pdbsite=CO1:So4+Binding+Site+For+Chain+A'>CO1</scene> | |SITE= <scene name='pdbsite=CO1:So4+Binding+Site+For+Chain+A'>CO1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> | + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1obx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1obx OCA], [http://www.ebi.ac.uk/pdbsum/1obx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1obx RCSB]</span> | ||
}} | }} | ||
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[[Category: Devedjiev, Y.]] | [[Category: Devedjiev, Y.]] | ||
[[Category: Kang, B S.]] | [[Category: Kang, B S.]] | ||
| - | [[Category: CO]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: nuclear protein]] | ||
[[Category: pdz domain]] | [[Category: pdz domain]] | ||
| - | [[Category: signal transduction]] | + | [[Category: signal transduction,nuclear protein,]] |
| - | ''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 22:43:01 2008'' |
Revision as of 19:43, 30 March 2008
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| , resolution 1.35Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH AN INTERLEUKIN 5 RECEPTOR ALPHA PEPTIDE.
Overview
Crystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5 receptor (alpha chain) and syndecan, reveal the molecular roots of syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the syndecan interaction as class II (-phi-X-phi). These results, in conjunction with other emerging structural data on PDZ domains, call for a revision of their classification and of the existing model of their mechanism.
About this Structure
1OBX is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm., Kang BS, Cooper DR, Devedjiev Y, Derewenda U, Derewenda ZS, Structure. 2003 Jul;11(7):845-53. PMID:12842047
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