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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-10-16
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pubmed:abstractText |
The FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three alpha helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third alpha helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
323
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
411-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12381297-Amino Acid Sequence,
pubmed-meshheading:12381297-Binding Sites,
pubmed-meshheading:12381297-Carrier Proteins,
pubmed-meshheading:12381297-Humans,
pubmed-meshheading:12381297-Models, Molecular,
pubmed-meshheading:12381297-Molecular Sequence Data,
pubmed-meshheading:12381297-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12381297-Phosphopeptides,
pubmed-meshheading:12381297-Protein Binding,
pubmed-meshheading:12381297-Protein Conformation,
pubmed-meshheading:12381297-Protein Folding,
pubmed-meshheading:12381297-Protein Structure, Tertiary,
pubmed-meshheading:12381297-Sequence Alignment
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pubmed:year |
2002
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pubmed:articleTitle |
The structure of an FF domain from human HYPA/FBP11.
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pubmed:affiliation |
MRC Centre for Protein Engineering, Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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