Coordinating the impact of structural genomics on the human [alpha]-helical transmembrane proteome

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 mor...

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Veröffentlicht in:Nature structural & molecular biology 2013-02, Vol.20 (2), p.135
Hauptverfasser: Pieper, Ursula, Schlessinger, Avner, Kloppmann, Edda, Chang, Geoffrey A, Chou, James J, Dumont, Mark E, Fox, Brian G, Fromme, Petra, Hendrickson, Wayne A, Malkowski, Michael G, Rees, Douglas C, Stokes, David L, Stowell, Michael H B, Wiener, Michael C, Rost, Burkhard, Stroud, Robert M, Stevens, Raymond C, Sali, Andrej
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Sprache:eng
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Zusammenfassung: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.
ISSN:1545-9993
1545-9985
DOI:10.1038/nsmb.2508