1N99: Crystal Structure Of The Pdz Tandem Of Human Syntenin

Syntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II. We report a crystal structure of the functional fragment of human syntenin containing two canonical PDZ domains, as well as binding studies for full-length syntenin, the PDZ tandem, and isolated PDZ domains. We show that the functional properties of syntenin are a result of independent interactions with target peptides, and that each domain is able to bind peptides belonging to two different classes: PDZ1 binds peptides from classes I and III, while PDZ2 interacts with classes I and II. The independent binding of merlin by PDZ1 and syndecan-4 by PDZ2 provides direct evidence for the coupling of syndecan-mediated signaling to actin regulation by merlin.
PDB ID: 1N99Download
MMDB ID: 22677
PDB Deposition Date: 2002/11/22
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.94  Å
Source Organism:
Similar Structures:
Biological Unit for 1N99: dimeric; determined by author and by software (PISA)
Molecular Components in 1N99
Label Count Molecule
Proteins (2 molecules)
Syntenin 1(Gene symbol: SDCBP)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB