CCRXP: exploring clusters of conserved residues in protein structures

被引:12
作者
Ahmad, Shandar [1 ]
Keskin, Ozlem [2 ]
Mizuguchi, Kenji [1 ]
Sarai, Akinori [3 ]
Nussinov, Ruth [4 ,5 ]
机构
[1] Natl Inst Biomed Innovat, Osaka 5670085, Japan
[2] Koc Univ, Coll Engn, Ctr Computat Biol & Bioinformat, TR-34450 Sariyer, Turkey
[3] Kyushu Inst Technol, Dept Biosci & Bioinformat, Fukuoka 8208502, Japan
[4] Tel Aviv Univ, Sackler Fac Med, Dept Human Genet & Mol Med, Tel Aviv, Israel
[5] NCI, Ctr Canc Res Nanobiol Program, SAIC Fredrick, Frederick, MD 21701 USA
基金
美国国家卫生研究院;
关键词
COMPUTATIONAL HOT-SPOTS; DNA-BINDING PROTEINS; INTERFACES; DATABASE; ARCHIVE;
D O I
10.1093/nar/gkq360
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
Conserved residues forming tightly packed clusters have been shown to be energy hot spots in both protein-protein and protein-DNA complexes. A number of analyses on these clusters of conserved residues (CCRs) have been reported, all pointing to a crucial role that these clusters play in protein function, especially protein-protein and protein-DNA interactions. However, currently there is no publicly available tool to automatically detect such clusters. Here, we present a web server that takes a coordinate file in PDB format as input and automatically executes all the steps to identify CCRs in protein structures. In addition, it calculates the structural properties of each residue and of the CCRs. We also present statistics to show that CCRs, determined by these procedures, are significantly enriched in 'hot spots' in protein-protein and protein-RNA complexes, which supplements our more detailed similar results on protein-DNA complexes. We expect that CCRXP web server will be useful in studies of protein structures and their interactions and selecting mutagenesis targets. The web server can be accessed at http://ccrxp.netasa.org.
引用
收藏
页码:W398 / W401
页数:4
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