Literature DB >> 9241427

The structural and functional basis of antibody catalysis.

H Wade1, T S Scanlan.   

Abstract

Ten years have passed since the initial reports that antibodies could be programmed to have enzymatic activity by immunization with a transition-site analog. Much of the research over the last decade has focused on defining the scope and generality of antibody catalysis; however, during the past two years the first few crystal structures of catalytic antibody transition-state analogs have been reported. This review analyzes four such structures of catalytic antibodies that catalyze markedly different reactions, including ester hydrolysis, sulfide oxidation, and a pericyclic rearrangement. Structure-function relations for these catalysts are discussed and compared to the structure and function of natural enzymes, as well as the chemistry that occurs in solution.

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Year:  1997        PMID: 9241427     DOI: 10.1146/annurev.biophys.26.1.461

Source DB:  PubMed          Journal:  Annu Rev Biophys Biomol Struct        ISSN: 1056-8700


  3 in total

1.  A glycosidase antibody elicited against a chair-like transition state analog by in vitro immunization.

Authors:  J Yu; S Y Choi; K D Moon; H H Chung; H J Youn; S Jeong; H Park; P G Schultz
Journal:  Proc Natl Acad Sci U S A       Date:  1998-03-17       Impact factor: 11.205

2.  De novo designed cyclic-peptide heme complexes.

Authors:  Michael M Rosenblatt; Jiangyun Wang; Kenneth S Suslick
Journal:  Proc Natl Acad Sci U S A       Date:  2003-10-31       Impact factor: 11.205

3.  The production of antibody fragments and antibody fusion proteins by yeasts and filamentous fungi.

Authors:  Vivi Joosten; Christien Lokman; Cees AMJJ Van Den Hondel; Peter J Punt
Journal:  Microb Cell Fact       Date:  2003-01-30       Impact factor: 5.328

  3 in total

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