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

doi:10.1038/nsmb.2508

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

Informatics 12 - Chair of Bioinformatics

Research output: Contribution to journal › Review article › peer-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 language	English
Pages (from-to)	135-138
Number of pages	4
Journal	Nature Structural and Molecular Biology
Volume	20
Issue number	2
DOIs	https://doi.org/10.1038/nsmb.2508
State	Published - Feb 2013

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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

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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.",

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

year = "2013",

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Pieper, U, Schlessinger, A, Kloppmann, E, Chang, GA, Chou, JJ, Dumont, ME, Fox, BG, Fromme, P, Hendrickson, WA, Malkowski, MG, Rees, DC, Stokes, DL, Stowell, MHB, Wiener, MC, Rost, B, Stroud, RM, Stevens, RC & Sali, A 2013, 'Coordinating the impact of structural genomics on the human α-helical transmembrane proteome', Nature Structural and Molecular Biology, vol. 20, no. 2, pp. 135-138. https://doi.org/10.1038/nsmb.2508

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T1 - Coordinating the impact of structural genomics on the human α-helical transmembrane proteome

AU - Pieper, Ursula

AU - Schlessinger, Avner

AU - Kloppmann, Edda

AU - Chang, Geoffrey A.

AU - Chou, James J.

AU - Dumont, Mark E.

AU - Fox, Brian G.

AU - Fromme, Petra

AU - Hendrickson, Wayne A.

AU - Malkowski, Michael G.

AU - Rees, Douglas C.

AU - Stokes, David L.

AU - Stowell, Michael H.B.

AU - Wiener, Michael C.

AU - Rost, Burkhard

AU - Stroud, Robert M.

AU - Stevens, Raymond C.

AU - Sali, Andrej

PY - 2013/2

Y1 - 2013/2

N2 - 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.

AB - 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.

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DO - 10.1038/nsmb.2508

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SP - 135

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JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 2

ER -

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

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