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SCOP Database in 2002: Refinements Accommodate Structural Genomics

Overview
Specialty Biochemistry
Date 2001 Dec 26
PMID 11752311
Citations 147
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Abstract

The SCOP (Structural Classification of Proteins) database is a comprehensive ordering of all proteins of known structure, according to their evolutionary and structural relationships. Protein domains in SCOP are grouped into species and hierarchically classified into families, superfamilies, folds and classes. Recently, we introduced a new set of features with the aim of standardizing access to the database, and providing a solid basis to manage the increasing number of experimental structures expected from structural genomics projects. These features include: a new set of identifiers, which uniquely identify each entry in the hierarchy; a compact representation of protein domain classification; a new set of parseable files, which fully describe all domains in SCOP and the hierarchy itself. These new features are reflected in the ASTRAL compendium. The SCOP search engine has also been updated, and a set of links to external resources added at the level of domain entries. SCOP can be accessed at http://scop.mrc-lmb.cam.ac.uk/scop.

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References
1.
van den Ent F, Lockhart A, Kendrick-Jones J, Lowe J . Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning. Structure. 1999; 7(10):1181-7. DOI: 10.1016/s0969-2126(00)80052-0. View

2.
Karplus K, Barrett C, Hughey R . Hidden Markov models for detecting remote protein homologies. Bioinformatics. 1999; 14(10):846-56. DOI: 10.1093/bioinformatics/14.10.846. View

3.
FITCH W . Homology a personal view on some of the problems. Trends Genet. 2000; 16(5):227-31. DOI: 10.1016/s0168-9525(00)02005-9. View

4.
Hopfner K, Karcher A, Shin D, Craig L, Arthur L, Carney J . Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell. 2000; 101(7):789-800. DOI: 10.1016/s0092-8674(00)80890-9. View

5.
Lerman J, Robblee J, Fairman R, Hughson F . Structural analysis of the neuronal SNARE protein syntaxin-1A. Biochemistry. 2000; 39(29):8470-9. DOI: 10.1021/bi0003994. View