Return
Transmembrane protein structures without X-rays
DOI:10.1016/j.tibs.2005.12.005.png)
Abstract
En 中文
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.
Keywords:
3-DIMENSIONAL STRUCTURE
MEMBRANE-PROTEINS
ELECTRON-MICROSCOPY
LACTOSE PERMEASE
ESCHERICHIA-COLI
TRANSPORTER EMRE
MOLECULAR-BASIS
ALPHA-HELICES
GXXXG MOTIF
MODEL
Journal
IF:
11
Papers:
6.6K
Citations:
2.0W
Organization
No organization information available
Cited Papers
An automatic method for predicting transmembrane protein structures using cryo-EM and evolutionary data
BIOPHYSICAL JOURNAL
IF3.1

