1KWA

HUMAN CASK/LIN-2 PDZ DOMAIN

Summary for 1KWA

• Entry DOI: 10.2210/pdb1kwa/pdb
• Descriptor: HCASK/LIN-2 PROTEIN, SULFATE ION (3 entities in total)
• Functional Keywords: pdz domain, neurexin, syndecan, receptor clustering, kinase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (By similarity): O14936
• Total number of polymer chains: 2
• Total formula weight: 20677.93

Authors

Daniels, D.L.,Cohen, A.R.,Anderson, J.M.,Brunger, A.T. (deposition date: 1998-01-16, release date: 1998-05-27, Last modification date: 2024-02-14)

Primary citation

Daniels, D.L.,Cohen, A.R.,Anderson, J.M.,Brunger, A.T.
Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
Nat.Struct.Biol., 5:317-325, 1998

PubMed Abstract: PDZ domain containing proteins assist formation of cell-cell junctions and localization of membrane protein receptors and ion channels. PDZ domains interact with the C-terminal residues of a particular target membrane protein. Based on their binding specificities and sequence homologies, PDZ domains fall into two classes. The first crystal structure of a class II PDZ domain, that of hCASK, has been solved by multi-wavelength anomalous dispersion phasing. Complex formation with the C-terminus of a neighboring non-crystallographically related PDZ domain reveals interactions between hCASK and its ligand. Class II PDZ domains differ from class I domains by formation of a second hydrophobic binding pocket. The C-terminal carboxylate binding loop of the PDZ domain is structurally conserved in both classes suggesting a generalized carboxylate binding motif (h-Gly-h) where h is a hydrophobic residue.

PubMed: 9546224
DOI: 10.1038/nsb0498-317

Experimental method

X-RAY DIFFRACTION (1.93 Å)