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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Circular Dichroism
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Conserved Sequence / genetics
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Fatty Acid-Binding Proteins
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Fungal Proteins / chemistry*
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Fungal Proteins / genetics
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Mice
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Models, Molecular
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Molecular Sequence Data
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Molecular Weight
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Mutagenesis, Site-Directed / genetics
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Nuclear Magnetic Resonance, Biomolecular
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Peptide Fragments / chemistry*
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Peptide Fragments / genetics
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Saccharomyces cerevisiae / chemistry*
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Saccharomyces cerevisiae / genetics
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Sequence Alignment
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Thermodynamics
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Ultracentrifugation
Substances
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Carrier Proteins
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Fatty Acid-Binding Proteins
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Fnbp1 protein, mouse
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Fungal Proteins
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Peptide Fragments
Associated data
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PDB/1E0L
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PDB/1E0M
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PDB/1E0N