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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1999-6-10
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pubmed:databankReference |
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pubmed:abstractText |
Camelid serum contains a large fraction of functional heavy-chain antibodies - homodimers of heavy chains without light chains. The variable domains of these heavy-chain antibodies (VHH) have a long complementarity determining region 3 (CDR3) loop that compensates for the absence of the antigen-binding loops of the variable light chains (VL). In the case of the VHH fragment cAb-Lys3, part of the 24 amino acid long CDR3 loop protrudes from the antigen-binding surface and inserts into the active-site cleft of its antigen, rendering cAb-Lys3 a competitive enzyme inhibitor.
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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 |
Apr
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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 |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
361-70
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10196124-Amino Acid Sequence,
pubmed-meshheading:10196124-Animals,
pubmed-meshheading:10196124-Antibody Affinity,
pubmed-meshheading:10196124-Antibody Specificity,
pubmed-meshheading:10196124-Antigen-Antibody Complex,
pubmed-meshheading:10196124-Antigen-Antibody Reactions,
pubmed-meshheading:10196124-Binding Sites, Antibody,
pubmed-meshheading:10196124-Camels,
pubmed-meshheading:10196124-Cattle,
pubmed-meshheading:10196124-Crystallography, X-Ray,
pubmed-meshheading:10196124-Humans,
pubmed-meshheading:10196124-Immunoglobulin Heavy Chains,
pubmed-meshheading:10196124-Mice,
pubmed-meshheading:10196124-Models, Molecular,
pubmed-meshheading:10196124-Molecular Sequence Data,
pubmed-meshheading:10196124-Pancreas,
pubmed-meshheading:10196124-Protein Conformation,
pubmed-meshheading:10196124-Ribonuclease, Pancreatic,
pubmed-meshheading:10196124-Software,
pubmed-meshheading:10196124-Species Specificity
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pubmed:year |
1999
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pubmed:articleTitle |
A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops.
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pubmed:affiliation |
Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B-1640 St. Genesius-Rode, Belgium. klaas@ultr.vub.ac.be
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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