標題: Evolutionary information hidden in a single protein structure
作者: Shih, Chien-Hua
Chang, Chih-Min
Lin, Yeong-Shin
Lo, Wei-Cheng
Hwang, Jenn-Kang
生物資訊及系統生物研究所
Institude of Bioinformatics and Systems Biology
關鍵字: protein structure;sequence conservation;contact number;evolution;B-factors
公開日期: 1-六月-2012
摘要: The knowledge of conserved sequences in proteins is valuable in identifying functionally or structurally important residues. Generating the conservation profile of a sequence requires aligning families of homologous sequences and having knowledge of their evolutionary relationships. Here, we report that the conservation profile at the residue level can be quantitatively derived from a single protein structure with only backbone information. We found that the reciprocal packing density profiles of protein structures closely resemble their sequence conservation profiles. For a set of 554 nonhomologous enzymes, 74% (408/554) of the proteins have a correlation coefficient > 0.5 between these two profiles. Our results indicate that the three-dimensional structure, instead of being a mere scaffold for positioning amino acid residues, exerts such strong evolutionary constraints on the residues of the protein that its profile of sequence conservation essentially reflects that of its structural characteristics. Proteins 2012;. (c) 2012 Wiley Periodicals, Inc.
URI: http://hdl.handle.net/11536/15956
ISSN: 0887-3585
期刊: PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume: 80
Issue: 6
結束頁: 1647
顯示於類別:期刊論文


文件中的檔案:

  1. 000303759000011.pdf