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rdf:type |
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lifeskim:mentions |
umls-concept:C0003250,
umls-concept:C0019704,
umls-concept:C0021031,
umls-concept:C0242808,
umls-concept:C0439855,
umls-concept:C0444626,
umls-concept:C0596448,
umls-concept:C1136102,
umls-concept:C1413246,
umls-concept:C1826471,
umls-concept:C1837441
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pubmed:issue |
5
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pubmed:dateCreated |
1999-4-29
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pubmed:abstractText |
The crystal structure of an intact molecule of HIV-1 capsid protein (p24) in complex with a monoclonal antibody fragment recognizing an epitope on the C-terminal domain has been determined at 3 A resolution. The helical N- and C-terminal domains of p24 are linked by an extended peptide forming a flexibly linked dumb-bell-shaped molecule 75 A in overall length. The p24 construct used is a variant with an N-terminal extension that mimics to some extent the Gag context of p24. We observed a novel head-to-tail dimer of p24 molecules which occurs through the formation of a substantial intermolecular interface between the N- and C-terminal domains. Comparison with previously observed p24 dimers shows that the same residues and secondary structural elements can partake in different interfaces revealing a remarkable stickiness and plasticity of the p24 molecule, properties which, combined with the inter-domain flexibility, are presumably important in the assembly and maturation of viral particles. Previous mutagenesis studies designed to test specific N-N and C-C homodimer interfaces do not discriminate fully against the possibility of the observed N-C interface.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-2124709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-7685414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-7815527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-7966609,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-7969494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-7969495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-8251747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-8315575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-8662505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-8784350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-8980222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-8980234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9223641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9346481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9368755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9370371,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9499062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9501077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9525604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9573230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9636143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9696871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9699611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9813197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10064580-9931251
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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 |
Mar
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1124-36
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10064580-Amino Acid Sequence,
pubmed-meshheading:10064580-Antibodies, Monoclonal,
pubmed-meshheading:10064580-Crystallography, X-Ray,
pubmed-meshheading:10064580-Dimerization,
pubmed-meshheading:10064580-HIV Core Protein p24,
pubmed-meshheading:10064580-Immunoglobulin Fab Fragments,
pubmed-meshheading:10064580-Models, Molecular,
pubmed-meshheading:10064580-Molecular Sequence Data,
pubmed-meshheading:10064580-Protein Structure, Secondary,
pubmed-meshheading:10064580-Sequence Alignment,
pubmed-meshheading:10064580-Viral Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Head-to-tail dimers and interdomain flexibility revealed by the crystal structure of HIV-1 capsid protein (p24) complexed with a monoclonal antibody Fab.
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pubmed:affiliation |
European Molecular Laboratory Biology, Grenoble Outstation, B.P.156X, F-38042 Grenoble Cedex 9, France.
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pubmed:publicationType |
Journal Article
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