title: Transmembrane protein structures without X-rays.
abstract: Transmembrane (TM) proteins constitute 15-30% of the genome, but <1% of the structures in the Protein Data Bank. This discrepancy is disturbing, and emphasizes that structure determination of TM proteins remains challenging. The challenge is greatest for proteins from eukaryotes, the structures of which remain intractable despite tremendous advances that have been made towards structure determination of bacterial TM proteins. Notably, >50% of the membrane protein families in eukaryotes lack bacterial homologs. Therefore, it is conceivable that many more years will elapse before high-resolution structures of eukaryotic TM proteins emerge. Until then, integrated approaches that combine biochemical and computational analyses with low-resolution structures are likely to have increasingly important roles in providing frameworks for the mechanistic understanding of membrane-protein structure and function.
authors.affiliation: Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv 69978, Israel.
authors.forename: Sarel J
authors.initials: SJ
authors.lastname: Fleishman
authors.forename: Vinzenz M
authors.initials: VM
authors.lastname: Unger
authors.forename: Nir
authors.initials: N
authors.lastname: Ben-Tal
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D020285:Cryoelectron Microscopy / Q000379:methods; D030562:Databases, Protein; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins