Publication Date:
1982-10-29
Description:
The three-dimensional structure of a penicillin-sensitive D-alanyl-carboxypeptidase-transpeptidase has been determined by x-ray crystallography to a resolution of 2.8 angstroms. The site of binding of the beta-lactam antibiotics penicillin and cephalosporin has been located. These findings constitute direct observation of the interaction of beta-lactams with a transpeptidase enzyme and establish the feasibility of defining the molecular stereochemistry of this interaction for purposes of drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, J A -- Moews, P C -- Knox, J R -- Frere, J M -- Ghuysen, J M -- AI-13364-05/AI/NIAID NIH HHS/ -- AI-16702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 29;218(4571):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123246" target="_blank"〉PubMed〈/a〉
Keywords:
Binding Sites
;
*Carboxypeptidases
;
*Cephalosporins
;
Crystallography
;
Models, Molecular
;
*Muramoylpentapeptide Carboxypeptidase
;
*Penicillins
;
Protein Conformation
;
X-Ray Diffraction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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