Linked Life Data

10993728

Source:http://linkedlifedata.com/resource/pubmed/id/10993728

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-10-17
pubmed:databankReference
pubmed:abstractText
The three-dimensional structure of a complex of an Fab from a murine IgG2b(lambda) antibody (NC10.14) with a high potency sweet tasting hap- ten, N-(p-cyanophenyl)-N'-(diphenylmethyl)-N"-(carboxymethyl)guan idine (NC174), has been determined to 2.6 A resolution by X-ray crystallography. This complex crystallized in the triclinic space group P1, with two molecules in the asymmetric unit. In contrast to a companion monoclonal antibody (NC6.8) with a kappa-type light chain and similar high affinity for the NC174 ligand, the NC10.14 antibody possessed a large and deep antigen combining site bounded primarily by the third complementarity-determining regions (CDR3s) of the light and heavy chains. CDR3 of the heavy chain dominated the site and its crown protruded into the external solvent as a type 1' beta-turn. NC174 was nested against HCDR3 and was held in place by two tryptophan side-chains (L91 and L96) from LCDR3. The diphenyl rings were accommodated on an upper tier of the binding pocket that is largely hydrophobic. At the floor of the site, a positively charged arginine side-chain (H95) stabilized the orientation of the electronegative cyano group of the hapten. The negative charge on the acetate group was partially neutralized by a hydrogen bond with the phenolic hydroxyl group of tyrosine H58. Comparisons of the modes of binding of NC174 to the NC6.8 and NC10.14 antibodies illustrate the enormous structural and mechanistic diversity manifest by immune responses.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
302
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
853-72
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10993728-Amino Acid Sequence, pubmed-meshheading:10993728-Animals, pubmed-meshheading:10993728-Antibody Specificity, pubmed-meshheading:10993728-Antigen-Antibody Complex, pubmed-meshheading:10993728-Binding Sites, Antibody, pubmed-meshheading:10993728-Crystallography, X-Ray, pubmed-meshheading:10993728-Haptens, pubmed-meshheading:10993728-Humans, pubmed-meshheading:10993728-Hydrogen Bonding, pubmed-meshheading:10993728-Immunoglobulin Fragments, pubmed-meshheading:10993728-Immunoglobulin Heavy Chains, pubmed-meshheading:10993728-Immunoglobulin Light Chains, pubmed-meshheading:10993728-Ligands, pubmed-meshheading:10993728-Mice, pubmed-meshheading:10993728-Models, Molecular, pubmed-meshheading:10993728-Molecular Sequence Data, pubmed-meshheading:10993728-Protein Structure, Quaternary, pubmed-meshheading:10993728-Protein Structure, Secondary, pubmed-meshheading:10993728-Protein Structure, Tertiary, pubmed-meshheading:10993728-Sequence Alignment, pubmed-meshheading:10993728-Sweetening Agents
pubmed:year
2000
pubmed:articleTitle
The three-dimensional structure of a complex of a murine Fab (NC10. 14) with a potent sweetener (NC174): an illustration of structural diversity in antigen recognition by immunoglobulins.
pubmed:affiliation
Crystallography Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, 73104, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.