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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1997-12-4
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pubmed:abstractText |
Profilin, a ubiquitous low molecular weight (13,000-15,000 M(r)) actin binding protein, regulates the formation of F-actin structures in vivo, and is localized to specific cellular regions through interaction with proline-rich sequences. Here we report the 2.2 A X-ray structure of the complex between human platelet profilin (HPP) and a decamer of L-proline (L-Pro10). The L-Pro10 peptide adopts a left-handed type II poly-L-proline helix (PPII) and binds to a highly conserved patch of aromatic amino acids on the surface of profilin. The peptide and actin binding sites reside on orthogonal surfaces, and L-Pro10 binding does not result in a conformational rearrangement of HPP. This structure suggests a mechanism for the localization of profilin and its actin-related activities to sites of actin filament assembly in vivo.
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pubmed:commentsCorrections |
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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 |
Nov
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
953-60
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9360613-Amino Acid Sequence,
pubmed-meshheading:9360613-Binding Sites,
pubmed-meshheading:9360613-Blood Platelets,
pubmed-meshheading:9360613-Contractile Proteins,
pubmed-meshheading:9360613-Crystallography, X-Ray,
pubmed-meshheading:9360613-Cytoskeleton,
pubmed-meshheading:9360613-Humans,
pubmed-meshheading:9360613-Ligands,
pubmed-meshheading:9360613-Light,
pubmed-meshheading:9360613-Microfilament Proteins,
pubmed-meshheading:9360613-Models, Molecular,
pubmed-meshheading:9360613-Molecular Sequence Data,
pubmed-meshheading:9360613-Morphogenesis,
pubmed-meshheading:9360613-Oligopeptides,
pubmed-meshheading:9360613-Peptides,
pubmed-meshheading:9360613-Profilins,
pubmed-meshheading:9360613-Proline,
pubmed-meshheading:9360613-Protein Structure, Secondary,
pubmed-meshheading:9360613-Scattering, Radiation,
pubmed-meshheading:9360613-Sequence Alignment
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pubmed:year |
1997
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pubmed:articleTitle |
Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation.
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pubmed:affiliation |
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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