Structuring the universe of proteins

被引：44

作者：

Burley, SK ^{[1
]}

Bonanno, JB ^{[1
]}

机构：

[1] Rockefeller Univ, Howard Hughes Med Inst, Labs Mol Biophys, New York, NY 10021 USA

来源：

ANNUAL REVIEW OF GENOMICS AND HUMAN GENETICS | 2002年 / 3卷

关键词：

structural genomics; X-ray crystallography; NMR spectroscopy; bioinformatics; homology modeling;

D O I：

10.1146/annurev.genom.3.022502.103227

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

High-throughput sequencing of human genomes and those of important model organisms (mouse, Drosophila melanogaster, Caenorhabditis elegans, fungi, archaea) and bacterial pathogens has laid the foundation for another "big science" initiative in biology. Together, X-ray crystallographers, nuclear magnetic resonance (NMR) spectroscopists, and computational biologists are pursuing high-throughput structural studies aimed at developing a comprehensive three-dimensional view of the protein structure universe. The new science of structural genomics promises more than 10,000 experimental protein structures and millions of calculated homology models of related proteins. The evolutionary underpinnings and technological challenges of automating target selection, protein expression and purification, sample preparation, NMR and X-ray data measurement/analysis, homology modeling, and structure/function annotation are discussed in detail. An informative case study from one of the structural genomics centers funded by the National Institutes of Health and the National Institute of General Medical Sciences (NIH/NIGMS) demonstrates how this experimental/computational pipeline will reveal important links between form and function in biology and provide new insights into evolution and human health and disease.

引用

页码：243 / 262

页数：24

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