1Z86
Solution structure of the PDZ domain of alpha-syntrophin
Summary for 1Z86
| Entry DOI | 10.2210/pdb1z86/pdb |
| Related | 1Z87 |
| Descriptor | Alpha-1-syntrophin (1 entity in total) |
| Functional Keywords | two alpha helix, six beta strands, protein binding |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side: Q61234 |
| Total number of polymer chains | 1 |
| Total formula weight | 9384.88 |
| 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 citation | Yan, 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: 16252003DOI: 10.1038/sj.emboj.7600858 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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