Progress in structure prediction of α-helical membrane proteins

Sarel J. Fleishman*, Nir Ben-Tal

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

Abstract

Transmembrane (TM) proteins comprise 20-30% of the genome but, because of experimental difficulties, they represent less than 1% of the Protein Data Bank. The dearth of membrane protein structures makes computational prediction a potentially important means of obtaining novel structures. Recent advances in computational methods have been combined with experimental data to constrain the modeling of three-dimensional structures. Furthermore, threading and ab initio modeling approaches that were effective for soluble proteins have been applied to TM domains. Surprisingly, experimental structures, proteomic analyses and bioinformatics have revealed unexpected architectures that counter long-held views on TM protein structure and stability. Future computational and experimental studies aimed at understanding the thermodynamic and evolutionary bases of these architectural details will greatly enhance predictive capabilities.

Original languageEnglish
Pages (from-to)496-504
Number of pages9
JournalCurrent Opinion in Structural Biology
Volume16
Issue number4
DOIs
StatePublished - Aug 2006

Funding

FundersFunder number
Clore Israel Foundation
Israel Science Foundation

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