CAPRI: A Critical Assessment of PRedicted Interactions

被引:499
作者
Janin, J [1 ]
Henrick, K
Moult, J
Ten Eyck, L
Sternberg, MJE
Vajda, S
Vasker, I
Wodak, SJ
机构
[1] CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France
[2] EMBL, European Bioinformat Inst, Cambridge, England
[3] Univ Maryland, Maryland Biotechnol Inst, Ctr Adv Res Biotechnol, Rockville, MD 20850 USA
[4] UCSD 0505, San Diego Supercomp Ctr, La Jolla, CA USA
[5] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London, England
[6] Boston Univ, Boston, MA 02215 USA
[7] SUNY Stony Brook, Dept Appl Math & Stat, Bioinformat Lab, Stony Brook, NY 11794 USA
[8] Free Univ Brussels, Serv Conformat Macromol Biol & Bioinformat, Brussels, Belgium
关键词
protein-protein interaction; docking; blind prediction;
D O I
10.1002/prot.10381
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
CAPRI is a communitywide experiment to assess the capacity of protein-docking methods to predict protein-protein interactions. Nineteen groups participated in rounds I and 2 of CAPRI and submitted blind structure predictions for seven protein-protein complexes based on the known structure of the component proteins. The predictions were compared to the unpublished X-ray structures of the complexes. We describe here the motivations for launching CAPRI, the rules that we applied to select targets and run the experiment, and some conclusions that can already be drawn. The results stress the need for new scoring functions and for methods handling the conformation changes that were observed in some of the target systems. CAPRI has already been a powerful drive for the community of computational biologists who development docking algorithms. We hope that this issue of Proteins will also be of interest to the community of structural biologists, which we call upon to provide new targets for future rounds of CAPRI, and to all molecular biologists who view protein-protein recognition as an essential process. (C) 2003 Wiley-Liss, Inc.
引用
收藏
页码:2 / 9
页数:8
相关论文
共 37 条
[1]   An antibody that prevents the hemagglutinin low pH fusogenic transition [J].
Barbey-Martin, C ;
Gigant, B ;
Bizebard, T ;
Calder, LJ ;
Wharton, SA ;
Skehel, JJ ;
Knossow, M .
VIROLOGY, 2002, 294 (01) :70-74
[2]   The Protein Data Bank [J].
Berman, HM ;
Westbrook, J ;
Feng, Z ;
Gilliland, G ;
Bhat, TN ;
Weissig, H ;
Shindyalov, IN ;
Bourne, PE .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :235-242
[3]   PROTEIN-PROTEIN RECOGNITION ANALYZED BY DOCKING SIMULATION [J].
CHERFILS, J ;
DUQUERROY, S ;
JANIN, J .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1991, 11 (04) :271-280
[4]   Three Camelid VHH domains in complex with porcine pancreatic α-amylase -: Inhibition and versatility of binding topology [J].
Desmyter, A ;
Spinelli, S ;
Payan, F ;
Lauwereys, M ;
Wyns, L ;
Muyldermans, S ;
Cambillau, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (26) :23645-23650
[5]  
Dixon JS, 1997, PROTEINS, P198
[6]   X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr [J].
Fieulaine, S ;
Morera, S ;
Poncet, S ;
Mijakovic, I ;
Galinier, A ;
Janin, J ;
Deutscher, J ;
Nessler, S .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (21) :13437-13441
[7]  
Fischer D, 2001, PROTEINS, P171
[8]   SURFACE MOTIFS BY A COMPUTER VISION TECHNIQUE - SEARCHES, DETECTION, AND IMPLICATIONS FOR PROTEIN LIGAND RECOGNITION [J].
FISCHER, D ;
NOREL, R ;
WOLFSON, H ;
NUSSINOV, R .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1993, 16 (03) :278-292
[9]   Recent advances in structure-based rational drug design [J].
Gane, PJ ;
Dean, PM .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2000, 10 (04) :401-404
[10]   Functional organization of the yeast proteome by systematic analysis of protein complexes [J].
Gavin, AC ;
Bösche, M ;
Krause, R ;
Grandi, P ;
Marzioch, M ;
Bauer, A ;
Schultz, J ;
Rick, JM ;
Michon, AM ;
Cruciat, CM ;
Remor, M ;
Höfert, C ;
Schelder, M ;
Brajenovic, M ;
Ruffner, H ;
Merino, A ;
Klein, K ;
Hudak, M ;
Dickson, D ;
Rudi, T ;
Gnau, V ;
Bauch, A ;
Bastuck, S ;
Huhse, B ;
Leutwein, C ;
Heurtier, MA ;
Copley, RR ;
Edelmann, A ;
Querfurth, E ;
Rybin, V ;
Drewes, G ;
Raida, M ;
Bouwmeester, T ;
Bork, P ;
Seraphin, B ;
Kuster, B ;
Neubauer, G ;
Superti-Furga, G .
NATURE, 2002, 415 (6868) :141-147