Structure-Based Characterization of Multiprotein Complexes

被引:40
|
作者
Wiederstein, Markus [1 ]
Gruber, Markus [1 ]
Frank, Karl [1 ]
Melo, Francisco [2 ,3 ]
Sippl, Manfred J. [1 ]
机构
[1] Salzburg Univ, Dept Mol Biol, Div Struct Biol & Bioinformat, A-5020 Salzburg, Austria
[2] Pontificia Univ Catolica Chile, Fac Ciencias Biol, Dept Mol Genet & Microbiol, Santiago 8320000, Chile
[3] Millennium Inst Immunol & Immunotherapy, Mol Bioinformat Lab, Santiago 8320000, Chile
基金
奥地利科学基金会;
关键词
POLYMERASE PROCESSIVITY FACTOR; DNA-POLYMERASE; RIBOSOMAL-SUBUNIT; PROTEIN COMPLEXES; FOURIER SYNTHESIS; CRYSTAL-STRUCTURE; ATOMIC-STRUCTURE; TAILED PHAGES; SIMILARITY; TRANSCRIPTION;
D O I
10.1016/j.str.2014.05.005
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
Multiprotein complexes govern virtually all cellular processes. Their 3D structures provide important clues to their biological roles, especially through structural correlations among protein molecules and complexes. The detection of such correlations generally requires comprehensive searches in databases of known protein structures by means of appropriate structure-matching techniques. Here, we present a high-speed structure search engine capable of instantly matching large protein oligomers against the complete and up-to-date database of biologically functional assemblies of protein molecules. We use this tool to reveal unseen structural correlations on the level of protein quaternary structure and demonstrate its general usefulness for efficiently exploring complex structural relationships among known protein assemblies.
引用
收藏
页码:1063 / 1070
页数:8
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