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1Z87

solution structure of the split PH-PDZ Supramodule of alpha-Syntrophin

Summary for 1Z87
Entry DOI10.2210/pdb1z87/pdb
Related1Z86
NMR InformationBMRB: 6752
DescriptorAlpha-1-syntrophin (1 entity in total)
Functional Keywordsalpha-1-syntrophin, protein binding
Biological sourceMus musculus (house mouse)
Cellular locationCell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side: Q61234
Total number of polymer chains1
Total formula weight27716.32
Authors
Yan, J.,Xu, W.,Wen, W.,Long, J.F.,Adams, M.E.,Froehner, S.C.,Zhang, M. (deposition date: 2005-03-30, release date: 2006-01-24, Last modification date: 2024-05-29)
Primary citationYan, J.,Wen, W.,Xu, W.,Long, J.F.,Adams, M.E.,Froehner, S.C.,Zhang, M.
Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin
Embo J., 24:3985-3995, 2005
Cited by
PubMed Abstract: Pleckstrin homology (PH) domains play diverse roles in cytoskeletal dynamics and signal transduction. Split PH domains represent a unique subclass of PH domains that have been implicated in interactions with complementary partial PH domains 'hidden' in many proteins. Whether partial PH domains exist as independent structural units alone and whether two halves of a split PH domain can fold together to form an intact PH domain are not known. Here, we solved the structure of the PH(N)-PDZ-PH(C) tandem of alpha-syntrophin. The split PH domain of alpha-syntrophin adopts a canonical PH domain fold. The isolated partial PH domains of alpha-syntrophin, although completely unfolded, remain soluble in solution. Mixing of the two isolated domains induces de novo folding and yields a stable PH domain. Our results demonstrate that two complementary partial PH domains are capable of binding to each other to form an intact PH domain. We further showed that the PH(N)-PDZ-PH(C) tandem forms a functionally distinct supramodule, in which the split PH domain and the PDZ domain function synergistically in binding to inositol phospholipids.
PubMed: 16252003
DOI: 10.1038/sj.emboj.7600858
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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