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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
1997-6-19
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pubmed:abstractText |
Amphiphysin is an SH3 domain-containing neuronal protein that is highly concentrated in nerve terminals where it interacts via its SH3 domain with dynamin I, a GTPase implicated in synaptic vesicle endocytosis. We show here that the SH3 domain of amphiphysin, but not a mutant SH3 domain, bound with high affinity to a single site in the long proline-rich region of human dynamin I, that this site was distinct from the binding sites for other SH3 domains, and that the mutation of two adjacent amino acids in dynamin I was sufficient to abolish binding. The dynamin I sequence critically required for amphiphysin binding (PSRPNR) fits in the novel SH3 binding consensus identified for the SH3 domain of amphiphysin via a combinatorial peptide library approach: PXRPXR(H)R(H). Our data demonstrate that the long proline-rich stretch present in dynamin I contained multiple SH3 domain binding sites that recognize interacting proteins with high specificity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dynamin I,
http://linkedlifedata.com/resource/pubmed/chemical/Dynamins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/amphiphysin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
|
pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13419-25
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9148966-Amino Acid Sequence,
pubmed-meshheading:9148966-Animals,
pubmed-meshheading:9148966-Brain,
pubmed-meshheading:9148966-Dynamin I,
pubmed-meshheading:9148966-Dynamins,
pubmed-meshheading:9148966-GTP Phosphohydrolases,
pubmed-meshheading:9148966-Humans,
pubmed-meshheading:9148966-Molecular Sequence Data,
pubmed-meshheading:9148966-Nerve Tissue Proteins,
pubmed-meshheading:9148966-Proline,
pubmed-meshheading:9148966-Rabbits,
pubmed-meshheading:9148966-Sequence Analysis,
pubmed-meshheading:9148966-src Homology Domains
|
pubmed:year |
1997
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pubmed:articleTitle |
The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence.
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pubmed:affiliation |
Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, Boyer Center for Molecular Medicine, New Haven, Connecticut 06510, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|