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Title
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Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition.
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Authors
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D.L.Daniels,
A.R.Cohen,
J.M.Anderson,
A.T.Brünger.
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Ref.
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Nat Struct Biol, 1998,
5,
317-325.
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PubMed id
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Abstract
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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.
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