1ybo
From Proteopedia
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- | [[Image:1ybo.gif|left|200px]] | + | [[Image:1ybo.gif|left|200px]] |
- | + | ||
- | '''Crystal structure of the PDZ tandem of human syntenin with syndecan peptide''' | + | {{Structure |
+ | |PDB= 1ybo |SIZE=350|CAPTION= <scene name='initialview01'>1ybo</scene>, resolution 2.300Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= SDCBP, MDA9, SYCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of the PDZ tandem of human syntenin with syndecan peptide''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1YBO is a [ | + | 1YBO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBO OCA]. |
==Reference== | ==Reference== | ||
- | The binding of the PDZ tandem of syntenin to target proteins., Grembecka J, Cierpicki T, Devedjiev Y, Derewenda U, Kang BS, Bushweller JH, Derewenda ZS, Biochemistry. 2006 Mar 21;45(11):3674-83. PMID:[http:// | + | The binding of the PDZ tandem of syntenin to target proteins., Grembecka J, Cierpicki T, Devedjiev Y, Derewenda U, Kang BS, Bushweller JH, Derewenda ZS, Biochemistry. 2006 Mar 21;45(11):3674-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16533050 16533050] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: scaffolding protein]] | [[Category: scaffolding protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:20:48 2008'' |
Revision as of 13:20, 20 March 2008
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, resolution 2.300Å | |||||||
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Gene: | SDCBP, MDA9, SYCL (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the PDZ tandem of human syntenin with syndecan peptide
Overview
PDZ domains are among the most abundant protein modules in the known genomes. Their main function is to provide scaffolds for membrane-associated protein complexes by binding to the cytosolic, C-terminal fragments of receptors, channels, and other integral membrane proteins. Here, using both heteronuclear NMR and single crystal X-ray diffraction, we show how peptides with different sequences, including those corresponding to the C-termini of syndecan, neurexin, and ephrin B, can simultaneously bind to both PDZ domains of the scaffolding protein syntenin. The PDZ2 domain binds these peptides in the canonical fashion, and an induced fit mechanism allows for the accommodation of a range of side chains in the P(0) and P(-)(2) positions. However, binding to the PDZ1 domain requires that the target peptide assume a noncanonical conformation. These data help explain how syntenin, and perhaps other PDZ-containing proteins, may preferentially bind to dimeric and clustered targets, and provide a mechanistic explanation for the previously reported cooperative ligand binding by syntenin's two PDZ domains.
About this Structure
1YBO is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The binding of the PDZ tandem of syntenin to target proteins., Grembecka J, Cierpicki T, Devedjiev Y, Derewenda U, Kang BS, Bushweller JH, Derewenda ZS, Biochemistry. 2006 Mar 21;45(11):3674-83. PMID:16533050
Page seeded by OCA on Thu Mar 20 15:20:48 2008