Recent developments in membrane-protein structural genomics 英文参考文献.docVIP

Minireview Recent developments in membrane-protein structural genomics Fei Philip Gao and Timothy A Cross Address: Department of Chemistry and Biochemistry, and the National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310, USA. Correspondence: Fei Philip Gao. E-mail: gao@ Published: 3 January 2006 Genome Biology 2005, 6:244 (doi:10.1186/gb-2005-6-13-244) The electronic version of this article is the complete one and can be found online at /2005/6/13/244 ? 2005 BioMed Central Ltd Abstract Recent work has identified the topology of almost all the inner membrane proteins in Escherichia coli, and advances in nuclear magnetic resonance spectroscopy now allow the determination of ?-helical membrane protein structures at high resolution. Together these developments will help overcome the current limitations of high-throughput determination of membrane protein structures. The structural genomics initiatives now underway world- wide have the ultimate aim of determining the structures and functions of all proteins. The field has developed rapidly over the past five years and the rate at which struc- ture entries are being deposited in the public databases has increased significantly (Figure 1a). Structural genomics relies primarily on X-ray crystallography, nuclear magnetic resonance (NMR) and computational model building to determine protein structure. High-throughput operations for many of the processes involved have already been devel- oped, and the field is currently funded at a significant level in the United States, Canada, the European Union, Israel, China, and Japan. Genomic sequence analysis predicts that 20-30% of proteins produced by most organisms will be integral membrane proteins, which as a class are critical for many essential cellular functions and constitute 60-70% of current