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rdf:type |
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lifeskim:mentions |
umls-concept:C0031727,
umls-concept:C0034790,
umls-concept:C0035820,
umls-concept:C0205349,
umls-concept:C0282535,
umls-concept:C0439855,
umls-concept:C0444626,
umls-concept:C1145667,
umls-concept:C1167622,
umls-concept:C1514762,
umls-concept:C1705535,
umls-concept:C1744214,
umls-concept:C2349209,
umls-concept:C2825311
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pubmed:issue |
10
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pubmed:dateCreated |
1998-1-6
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pubmed:abstractText |
Human immunodeficiency virus (HIV) Nef protein accelerates virulent progression of acquired immunodeficiency syndrome (AIDS) by its interaction with specific cellular proteins involved in signal transduction and host cell activation. Nef has been shown to bind specifically to a subset of the Src family of kinases. The structures of free Nef and Nef bound to Src homology region 3 (SH3) domain are important for the elucidation of how the affinity and specificity for the Src kinase family SH3 domains are achieved, and also for the development of potential drugs and vaccines against AIDS.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/FYN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, nef,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fyn,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/nef Gene Products, Human...,
http://linkedlifedata.com/resource/pubmed/chemical/polyproline
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1361-72
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9351809-Amino Acid Sequence,
pubmed-meshheading:9351809-Conserved Sequence,
pubmed-meshheading:9351809-Crystallography, X-Ray,
pubmed-meshheading:9351809-Gene Products, nef,
pubmed-meshheading:9351809-HIV-1,
pubmed-meshheading:9351809-Humans,
pubmed-meshheading:9351809-Models, Molecular,
pubmed-meshheading:9351809-Molecular Sequence Data,
pubmed-meshheading:9351809-Peptides,
pubmed-meshheading:9351809-Protein Binding,
pubmed-meshheading:9351809-Protein Conformation,
pubmed-meshheading:9351809-Protein Structure, Secondary,
pubmed-meshheading:9351809-Proto-Oncogene Proteins,
pubmed-meshheading:9351809-Proto-Oncogene Proteins c-fyn,
pubmed-meshheading:9351809-Receptors, Antigen, T-Cell,
pubmed-meshheading:9351809-Sequence Alignment,
pubmed-meshheading:9351809-Signal Transduction,
pubmed-meshheading:9351809-T-Lymphocytes,
pubmed-meshheading:9351809-nef Gene Products, Human Immunodeficiency Virus,
pubmed-meshheading:9351809-src Homology Domains
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pubmed:year |
1997
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pubmed:articleTitle |
The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling.
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pubmed:affiliation |
Centre de Biochimie Structurale, UMR C9955 CNRS, U414 INSERM, Université Montpellier I, Faculté de Pharmacie, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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