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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1991-7-10
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55706,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55707,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55708,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55709,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55710,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M55711,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M74139,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M74422,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M74423,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M74424
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pubmed:abstractText |
The structural features of mAb directed against the opiate morphine were analyzed by using competitive ligand analog-binding studies, examination of the V region amino acid sequence, and computer-aided molecular modeling of the fragment V region. The antibody response in BALB/c mice to morphine is relatively restricted, in that all of the mAb examined in this study contained the same lambda L chain and very similar H chain V regions. A three-dimensional model of the antimorphine-binding site was constructed by using computational and graphic display techniques. Each of the six complementary-determining regions was constructed by using fragment replacement methods employing canonical loop conformations of known "parent" structures. Experimental competitive ligand-binding data and theoretical modeling suggest that a charged glutamate residue at position H:50 and aromatic side chains of residues H:33W, H:47W, H:58F, H:95W, H:101iY, and L:91W are key features in ionic and hydrophobic interactions with the ligand. This study represents the first use of theoretical and experimental modeling techniques to describe the Ag-binding site of a mouse fragment V region containing a lambda L chain.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0022-1767
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
146
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4248-57
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2040800-Amino Acid Sequence,
pubmed-meshheading:2040800-Animals,
pubmed-meshheading:2040800-Antibodies, Monoclonal,
pubmed-meshheading:2040800-Base Sequence,
pubmed-meshheading:2040800-Binding, Competitive,
pubmed-meshheading:2040800-Binding Sites, Antibody,
pubmed-meshheading:2040800-Computers,
pubmed-meshheading:2040800-Female,
pubmed-meshheading:2040800-Immunoglobulin Variable Region,
pubmed-meshheading:2040800-Mice,
pubmed-meshheading:2040800-Mice, Inbred BALB C,
pubmed-meshheading:2040800-Models, Molecular,
pubmed-meshheading:2040800-Molecular Sequence Data,
pubmed-meshheading:2040800-Morphine
|
pubmed:year |
1991
|
pubmed:articleTitle |
Analysis of the binding site architecture of monoclonal antibodies to morphine by using competitive ligand binding and molecular modeling.
|
pubmed:affiliation |
Department of Pathology and Laboratory Medicine, University of Texas Health Science Center, Houston 77030.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|