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Coordinating the impact of structural genomics on the human α-helical transmembrane proteome
- 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 HB;
- Wiener, Michael C;
- Rost, Burkhard;
- Stroud, Robert M;
- Stevens, Raymond C;
- Sali, Andrej
- et al.
Published Web Location
https://doi.org/10.1038/nsmb.2508Abstract
With 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%, thus providing structure/function information not otherwise available.
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