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 article

51 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 (US)
Pages (from-to)135-138
Number of pages4
JournalNature Structural and Molecular Biology
Volume20
Issue number2
DOIs
StatePublished - Feb 1 2013

    Fingerprint

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Pieper, U., Schlessinger, A., Kloppmann, E., Chang, G. A., Chou, J. J., Dumont, M. E., Fox, B. G., Fromme, P., Hendrickson, W. A., Malkowski, M. G., Rees, D. C., Stokes, D. L., Stowell, M. H. B., Wiener, M. C., Rost, B., Stroud, R. M., Stevens, R. C., & Sali, A. (2013). Coordinating the impact of structural genomics on the human α-helical transmembrane proteome. Nature Structural and Molecular Biology, 20(2), 135-138. https://doi.org/10.1038/nsmb.2508