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ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins.

Abstract：

:The alpha/beta-hydrolase fold is characterized by a beta-sheet core of five to eight strands connected by alpha-helices to form a alpha/beta/alpha sandwich. In most of the family members the beta-strands are parallels, but some show an inversion in the order of the first strands, resulting in antiparallel orientation. The members of the superfamily diverged from a common ancestor into a number of hydrolytic enzymes with a wide range of substrate specificities, together with other proteins with no recognized catalytic activity. In the enzymes the catalytic triad residues are presented on loops, of which one, the nucleophile elbow, is the most conserved feature of the fold. Of the other proteins, which all lack from one to all of the catalytic residues, some may simply be 'inactive' enzymes while others are known to be involved in surface recognition functions. The ESTHER database (http://bioweb.ensam.inra.fr/esther) gathers and annotates all the published information related to gene and protein sequences of this superfamily, as well as biochemical, pharmacological and structural data, and connects them so as to provide the bases for studying structure-function relationships within the family. The most recent developments of the database, which include a section on human diseases related to members of the family, are described.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Hotelier T,Renault L,Cousin X,Negre V,Marchot P,Chatonnet A

doi

10.1093/nar/gkh141

keywords:

subject

Has Abstract

pub_date

2004-01-01 00:00:00

pages

D145-7

issue

Database issue

eissn

0305-1048

issn

1362-4962

pii

32/suppl_1/D145

journal_volume

32

pub_type

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