1E0M
PROTOTYPE WW domain
Summary for 1E0M
| Entry DOI | 10.2210/pdb1e0m/pdb |
| Related | 1E0L 1E0N |
| Descriptor | WWPROTOTYPE (1 entity in total) |
| Functional Keywords | sh3 prototype, wwprototype, protein design, de novo protein |
| Biological source | SYNTHETIC CONSTRUCT |
| Total number of polymer chains | 1 |
| Total formula weight | 4358.74 |
| Authors | Macias, M.J.,Gervais, V.,Civera, C.,Oschkinat, H. (deposition date: 2000-04-01, release date: 2000-04-20, Last modification date: 2024-05-15) |
| Primary citation | Macias, M.J.,Gervais, V.,Civera, C.,Oschkinat, H. Structural Analysis of Ww Domains and Design of a Ww Prototype Nat.Struct.Biol., 7:375-, 2000 Cited by PubMed Abstract: Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands. The structural roles of conserved residues have been studied using site-directed mutagenesis of both wild type domains. Crucial interactions responsible for the stability of the WW structure have been identified. Based on a network of highly conserved long range interactions across the beta-sheet structure that supports the WW fold and on a systematic analysis of conserved residues in the WW family, we have designed a folded prototype WW sequence. PubMed: 10802733DOI: 10.1038/75144 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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