Linked Life Data

9159478

Source:http://linkedlifedata.com/resource/pubmed/id/9159478

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-6-16
pubmed:abstractText
The crystal structure of the esterase catalytic antibody 48G7 has been determined in the presence of hapten at 2.0 A resolution and in the absence of hapten at 2.7 A resolution. The root-mean-square difference between the two structures is 0.6 A for the variable domain and 0.7 A for the constant domain. Comparison of the active site shows that no significant changes occur upon hapten binding as main-chain and side-chain displacements are negligible. Complex formation occurs as hapten fits into a pre-formed pocket about 10 A deep. Although 151 water molecules were modeled into the 48G7-hapten structure, none are bound in the active site. Comparison of the 48G7 structures with those of other published ester hydrolysis antibodies illustrates an emerging theme used by esterolytic antibodies in binding their (nitro-)phenyl haptens and in hydrolysing their cognate esters and carbonates: hapten is bound with the aryl end buried deep in the binding pocket, and the phosphonate moiety is responsible for the majority of the binding energy to the antibody-hapten interaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
390-400
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Crystal structures of the free and liganded form of an esterolytic catalytic antibody.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Chemistry, University of California, Berkeley 94720, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't