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

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: 10802733
DOI: 10.1038/75144

Experimental method

SOLUTION NMR