Coordinating the impact of structural genomics on the human α-helical transmembrane proteome

  • Ursula Pieper
  • , Avner Schlessinger
  • , Edda Kloppmann
  • , Geoffrey A. Chang
  • , James J. Chou
  • , Mark E. Dumont
  • , Brian G. Fox
  • , Petra Fromme
  • , Wayne A. Hendrickson
  • , Michael G. Malkowski
  • , Douglas C. Rees
  • , David L. Stokes
  • , Michael H.B. Stowell
  • , Michael C. Wiener
  • , Burkhard Rost
  • , Robert M. Stroud
  • , Raymond C. Stevens
  • , Andrej Sali

Research output: Contribution to journalReview articlepeer-review

55 Scopus citations

Abstract

Given the recent successes in determining membrane-protein structures, we explore the tractability of determining representatives for the entire human membrane proteome. This proteome contains 2,925 unique integral α-helical transmembrane-domain sequences that cluster into 1,201 families sharing more than 25% sequence identity. Structures of 100 optimally selected targets would increase the fraction of modelable human α-helical transmembrane domains from 26% to 58%, providing structure and function information not otherwise available.

Original languageEnglish
Pages (from-to)135-138
Number of pages4
JournalNature Structural and Molecular Biology
Volume20
Issue number2
DOIs
StatePublished - Feb 2013

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