SCOP database in 2004: refinements integrate structure and sequence family data

被引:721
作者
Andreeva, A
Howorth, D
Brenner, SE
Hubbard, TJP
Chothia, C
Murzin, AG
机构
[1] MRC, Ctr Prot Engn, Cambridge CB2 2QH, England
[2] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
[3] Univ Calif Berkeley, Dept Plant & Microbial Biol, Berkeley, CA 94720 USA
[4] Wellcome Trust Sanger Inst, Cambridge CB10 1SA, England
关键词
D O I
10.1093/nar/gkh039
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Structural Classification of Proteins (SCOP) database is a comprehensive ordering of all proteins of known structure, according to their evolutionary and structural relationships. Protein domains in SCOP are hierarchically classified into families, superfamilies, folds and classes. The continual accumulation of sequence and structural data allows more rigorous analysis and provides important information for understanding the protein world and its evolutionary repertoire. SCOP participates in a project that aims to rationalize and integrate the data on proteins held in several sequence and structure databases. As part of this project, starting with release 1.63, we have initiated a refinement of the SCOP classification, which introduces a number of changes mostly at the levels below superfamily. The pending SCOP reclassification will be carried out gradually through a number of future releases. In addition to the expanded set of static links to external resources, available at the level of domain entries, we have started modernization of the interface capabilities of SCOP allowing more dynamic links with other databases. SCOP can be accessed at http://scop.mrc-lmb.cam.ac.uk/scop.
引用
收藏
页码:D226 / D229
页数:4
相关论文
共 20 条
[1]  
Bateman A, 2004, NUCLEIC ACIDS RES, V32, pD138, DOI [10.1093/nar/gkp985, 10.1093/nar/gkr1065, 10.1093/nar/gkh121]
[2]   PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES [J].
BERNSTEIN, FC ;
KOETZLE, TF ;
WILLIAMS, GJB ;
MEYER, EF ;
BRICE, MD ;
RODGERS, JR ;
KENNARD, O ;
SHIMANOUCHI, T ;
TASUMI, M .
JOURNAL OF MOLECULAR BIOLOGY, 1977, 112 (03) :535-542
[3]  
Brenner SE, 1996, METHOD ENZYMOL, V266, P635
[4]   The ASTRAL Compendium in 2004 [J].
Chandonia, JM ;
Hon, G ;
Walker, NS ;
Lo Conte, L ;
Koehl, P ;
Levitt, M ;
Brenner, SE .
NUCLEIC ACIDS RESEARCH, 2004, 32 :D189-D192
[5]   The structure of tobacco ringspot virus: a link in the evolution of icosahedral capsids in the picornavirus superfamily [J].
Chandrasekar, V ;
Johnson, JE .
STRUCTURE, 1998, 6 (02) :157-171
[6]   E-MSD: an integrated data resource for bioinformatics [J].
Golovin, A ;
Oldfield, TJ ;
Tate, JG ;
Velankar, S ;
Barton, GJ ;
Boutselakis, H ;
Dimitropoulos, D ;
Fillon, J ;
Hussain, A ;
Ionides, JMC ;
John, M ;
Keller, PA ;
Krissinel, E ;
McNeil, P ;
Naim, A ;
Newman, R ;
Pajon, A ;
Pineda, J ;
Rachedi, A ;
Copeland, J ;
Sitnov, A ;
Sobhany, S ;
Suarez-Uruena, A ;
Swaminathan, GJ ;
Tagari, M ;
Tromm, S ;
Vranken, W ;
Henrick, K .
NUCLEIC ACIDS RESEARCH, 2004, 32 :D211-D216
[7]   Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure [J].
Gough, J ;
Karplus, K ;
Hughey, R ;
Chothia, C .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 313 (04) :903-919
[8]   Genomic analysis of the eukaryotic protein kinase superfamily: a perspective [J].
Hanks, SK .
GENOME BIOLOGY, 2003, 4 (05)
[9]   CRYSTAL-STRUCTURE OF AN ENDOTOXIN-NEUTRALIZING PROTEIN FROM THE HORSESHOE-CRAB, LIMULUS ANTI-LPS FACTOR, AT 1.5 ANGSTROM RESOLUTION [J].
HOESS, A ;
WATSON, S ;
SIBER, GR ;
LIDDINGTON, R .
EMBO JOURNAL, 1993, 12 (09) :3351-3356
[10]   Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12 [J].
Huse, M ;
Chen, YG ;
Massagué, J ;
Kuriyan, J .
CELL, 1999, 96 (03) :425-436