Transmembrane protein structures without X-rays

Sarel J. Fleishman, Vinzenz M. Unger, Nir Ben-Tal*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

72 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)106-113
Number of pages8
JournalTrends in Biochemical Sciences
Volume31
Issue number2
DOIs
StatePublished - Feb 2006

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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