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PROTEIN SUPERFAMILIES AND DOMAIN SUPERFOLDS
Author(s): ORENGO CA, JONES DT, THORNTON JM
Source: NATURE    Volume: 372    Issue: 6507    Pages: 631-634    Published: DEC 15 1994  
Times Cited: 517     References: 27     
Abstract: As the protein sequence and structure databases expand rapidly a better understanding of the relationships between proteins is required. A classification is considered that extends the sequence-based superfamilies to include proteins with similar function and three-dimensional structures but no sequence similarity. So far there are only nine protein folds known to recur in proteins having neither sequence nor functional similarity. These folds dominate the structure database, representing more than 30 per cent of all determined structures. This observation has implications for protein-fold recognition.
Document Type: Article
Language: English
Reprint Address: ORENGO, CA (reprint author), UNIV LONDON UNIV COLL, DEPT BIOCHEM & MOLEC BIOL, BIOMOLEC STRUCT & MODELLING UNIT, GOWER ST, LONDON WC1E 6BT, ENGLAND
Addresses:
1. NATL INST MED RES, MATH BIOL LAB, LONDON NW7 1AA, ENGLAND
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: PX307
ISSN: 0028-0836
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