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PROFESS: a PROtein function, evolution, structure and sequence database.PROFESS:蛋白质功能、进化、结构和序列数据库。
Database (Oxford). 2010 Jul 6;2010:baq011. doi: 10.1093/database/baq011.
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Considerations to improve functional annotations in biological databases.考虑改进生物数据库中的功能注释。
OMICS. 2009 Dec;13(6):527-35. doi: 10.1089/omi.2009.0075.
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Annotation error in public databases: misannotation of molecular function in enzyme superfamilies.公共数据库中的注释错误:酶超家族中分子功能的错误注释。
PLoS Comput Biol. 2009 Dec;5(12):e1000605. doi: 10.1371/journal.pcbi.1000605. Epub 2009 Dec 11.
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eggNOG v2.0: extending the evolutionary genealogy of genes with enhanced non-supervised orthologous groups, species and functional annotations.eggNOG v2.0:通过增强的非监督同源物聚类、物种和功能注释,扩展基因的进化系统发生。
Nucleic Acids Res. 2010 Jan;38(Database issue):D190-5. doi: 10.1093/nar/gkp951. Epub 2009 Nov 9.
5
Structure is three to ten times more conserved than sequence--a study of structural response in protein cores.结构的保守性比序列高出三到十倍——对蛋白质核心结构响应的研究。
Proteins. 2009 Nov 15;77(3):499-508. doi: 10.1002/prot.22458.
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Cross-over between discrete and continuous protein structure space: insights into automatic classification and networks of protein structures.离散与连续蛋白质结构空间之间的交叉:对蛋白质结构自动分类及网络的见解。
PLoS Comput Biol. 2009 Mar;5(3):e1000331. doi: 10.1371/journal.pcbi.1000331. Epub 2009 Mar 27.
7
Protein function prediction--the power of multiplicity.蛋白质功能预测——多样性的力量。
Trends Biotechnol. 2009 Apr;27(4):210-9. doi: 10.1016/j.tibtech.2009.01.002. Epub 2009 Feb 27.
8
The effect of sequence evolution on protein structural divergence.序列进化对蛋白质结构差异的影响。
Mol Biol Evol. 2009 May;26(5):1055-65. doi: 10.1093/molbev/msp020. Epub 2009 Feb 4.
9
Phylogenetic profiles reveal evolutionary relationships within the "twilight zone" of sequence similarity.系统发育谱揭示了序列相似性“模糊地带”内的进化关系。
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10
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细菌蛋白结构揭示门水平的分化。

Bacterial protein structures reveal phylum dependent divergence.

机构信息

Department of Chemistry, University of Nebraska-Lincoln, 68588-0304, United States.

出版信息

Comput Biol Chem. 2011 Feb;35(1):24-33. doi: 10.1016/j.compbiolchem.2010.12.004. Epub 2011 Jan 18.

DOI:10.1016/j.compbiolchem.2010.12.004
PMID:21315656
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3049983/
Abstract

Protein sequence space is vast compared to protein fold space. This raises important questions about how structures adapt to evolutionary changes in protein sequences. A growing trend is to regard protein fold space as a continuum rather than a series of discrete structures. From this perspective, homologous protein structures within the same functional classification should reveal a constant rate of structural drift relative to sequence changes. The clusters of orthologous groups (COG) classification system was used to annotate homologous bacterial protein structures in the Protein Data Bank (PDB). The structures and sequences of proteins within each COG were compared against each other to establish their relatedness. As expected, the analysis demonstrates a sharp structural divergence between the bacterial phyla Firmicutes and Proteobacteria. Additionally, each COG had a distinct sequence/structure relationship, indicating that different evolutionary pressures affect the degree of structural divergence. However, our analysis also shows the relative drift rate between sequence identity and structure divergence remains constant.

摘要

与蛋白质折叠空间相比,蛋白质序列空间是巨大的。这就提出了一个重要的问题,即结构如何适应蛋白质序列的进化变化。一种日益增长的趋势是将蛋白质折叠空间视为连续体,而不是离散结构的系列。从这个角度来看,同一功能分类内的同源蛋白质结构应该相对于序列变化显示出恒定的结构漂移速率。共同源群(COG)分类系统用于注释蛋白质数据库(PDB)中的同源细菌蛋白质结构。比较每个 COG 中的蛋白质结构和序列,以确定它们的相关性。正如预期的那样,该分析表明细菌门Firmicutes 和 Proteobacteria 之间存在明显的结构分歧。此外,每个 COG 都有独特的序列/结构关系,表明不同的进化压力会影响结构分歧的程度。然而,我们的分析还表明,序列同一性和结构分歧之间的相对漂移率保持不变。

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