期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 79, 期 -, 页码 6-20出版社
WILEY
DOI: 10.1002/prot.23196
关键词
CASP; protein structure; X-ray crystal-lography; NMR; structure prediction
资金
- National Library of Medicine (NIH/NLM) [LM007085]
- Spanish Ministry of Education and Science [BFU2008-01588]
- European Commission [NMP4-CT-2006-033256]
- Spanish Ministry of Education and Science
- Xunta de Galicia
- National Institutes of Health [K22-CA124517, R01-GM090161, GM074942, GM094585]
- U.S. Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- Foundation for Polish Science
- NSF [DBI 0829586]
- NATIONAL CANCER INSTITUTE [K22CA124517] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U54GM094585, R01GM100482, R01GM090161, U54GM074942] Funding Source: NIH RePORTER
- NATIONAL LIBRARY OF MEDICINE [P41LM007085] Funding Source: NIH RePORTER
- Direct For Biological Sciences [0829586] Funding Source: National Science Foundation
One goal of the CASP community wide experiment on the critical assessment of techniques for protein structure prediction is to identify the current state of the art in protein structure prediction and modeling. A fundamental principle of CASP is blind prediction on a set of relevant protein targets, that is, the participating computational methods are tested on a common set of experimental target proteins, for which the experimental structures are not known at the time of modeling. Therefore, the CASP experiment would not have been possible without broad support of the experimental protein structural biology community. In this article, several experimental groups discuss the structures of the proteins which they provided as prediction targets for CASP9, highlighting structural and functional peculiarities of these structures: the long tail fiber protein gp37 from bacteriophage T4, the cyclic GMP-dependent protein kinase I beta dimerization/docking domain, the ectodomain of the JTB (jumping translocation breakpoint) transmembrane receptor, Autotaxin in complex with an inhibitor, the DNA-binding J-binding protein 1 domain essential for biosynthesis and maintenance of DNA base-J (beta-D-glucosyl-hydroxymethyluracil) in Trypanosoma and Leishmania, an so far uncharacterized 73 residue domain from Ruminococcus gnavus with a fold typical for PDZ-like domains, a domain from the phycobilisome core-membrane linker phycobiliprotein ApcE from Synechocystis, the heat shock protein 90 activators PFC0360w and PFC0270w from Plasmodium falciparum, and 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae. Proteins 2011; 79(Suppl 10):6-20. (C) 2011 Wiley-Liss, Inc.
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