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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1991-5-17
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pubmed:abstractText |
Comparison between the structures and solvent-accessible surfaces of the antigen-binding fragments of two murine anti-p-azophenylarsonate monoclonal antibodies, one bearing a major cross-reactive idiotype of A/J strain mice (36-71) and one lacking the idiotype (R19.9; Lascombe et al., 1989), highlight the structural basis for the determination of hapten affinity and idiotypy. Since the sequence of R 19.9 is identical with the germline-encoded sequence at 16 positions in both heavy-chain and light-chain variable regions where somatic mutations and junctional differences have occurred to produce the 36-71 sequence, the structure of R 19.9 can be used to model the structure of the germline-encoded antibody (36-65) in the regions around these sites. These 16 sequence differences exclude the third heavy-chain complementarity-determining region because R 19.9 utilizes a D gene segment not associated with the predominant idiotype, which is 4 residues longer than the canonical D gene segment utilized in the sequences of 36-71 and 36-65. This difference between the structures of R 19.9 and 36-71 does not affect the validity of using the structure of R 19.9 to model the structure of 36-65 since the third heavy-chain complementarity-determining region is highly solvent-exposed in both 36-71 and R 19.9, and does not interact with any of these 16 sites. Comparing the structures of 36-71 and R 19.9 suggests that only three of the differences in the heavy-chain sequences, and three of the differences in the light-chain sequences of 36-71 and 36-65, increase the affinity for hapten.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Haptens,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Constant Regions,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fab Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Idiotypes,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Variable Region,
http://linkedlifedata.com/resource/pubmed/chemical/p-Azobenzenearsonate
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3749-57
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2015230-Amino Acid Sequence,
pubmed-meshheading:2015230-Animals,
pubmed-meshheading:2015230-Antibodies, Monoclonal,
pubmed-meshheading:2015230-Haptens,
pubmed-meshheading:2015230-Immunoglobulin Constant Regions,
pubmed-meshheading:2015230-Immunoglobulin Fab Fragments,
pubmed-meshheading:2015230-Immunoglobulin Idiotypes,
pubmed-meshheading:2015230-Immunoglobulin Variable Region,
pubmed-meshheading:2015230-Models, Molecular,
pubmed-meshheading:2015230-Molecular Sequence Data,
pubmed-meshheading:2015230-Protein Conformation,
pubmed-meshheading:2015230-Stereoisomerism,
pubmed-meshheading:2015230-Temperature,
pubmed-meshheading:2015230-p-Azobenzenearsonate
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pubmed:year |
1991
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pubmed:articleTitle |
Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 2. Structural basis of hapten binding and idiotypy.
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pubmed:affiliation |
California Institute of Technology, Pasadena 91125.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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