1nte
From Proteopedia
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|PDB= 1nte |SIZE=350|CAPTION= <scene name='initialview01'>1nte</scene>, resolution 1.24Å | |PDB= 1nte |SIZE=350|CAPTION= <scene name='initialview01'>1nte</scene>, resolution 1.24Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=O:OXYGEN ATOM'>O</scene> | + | |LIGAND= <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SDCBP OR MDA9 OR SYCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SDCBP OR MDA9 OR SYCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1n99|1N99]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nte OCA], [http://www.ebi.ac.uk/pdbsum/1nte PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nte RCSB]</span> | ||
}} | }} | ||
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[[Category: Devedjiev, Y.]] | [[Category: Devedjiev, Y.]] | ||
[[Category: Kang, B S.]] | [[Category: Kang, B S.]] | ||
| - | [[Category: O]] | ||
[[Category: pdz recognition]] | [[Category: pdz recognition]] | ||
[[Category: syntenin]] | [[Category: syntenin]] | ||
| - | ''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 22:35:15 2008'' |
Revision as of 19:35, 30 March 2008
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| , resolution 1.24Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SDCBP OR MDA9 OR SYCL (Homo sapiens) | ||||||
| Related: | 1N99
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE ANALYSIS OF THE SECOND PDZ DOMAIN OF SYNTENIN
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
1NTE is a Single protein structure of sequence 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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