1w9e: Difference between revisions
No edit summary |
No edit summary |
||
| Line 25: | Line 25: | ||
[[Category: scaffolding protein signaling protein]] | [[Category: scaffolding protein signaling protein]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:29:02 2007'' | ||
Revision as of 17:24, 30 October 2007
|
CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN IN COMPLEX WITH TNEFYF PEPTIDE
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1W9E is a [Single protein] structure of sequence from [Homo sapiens] with BEZ as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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 Tue Oct 30 16:29:02 2007