A de novo peptide hexamer with a mutable channel.
A de novo peptide hexamer with a mutable channel.
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DOI:
10.1038/nchembio.692
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发表时间:
2011-10-30
影响因子:
14.8
通讯作者:
Woolfson, Derek N.
中科院分区:
文献类型:
--
作者:
Zaccai, Nathan R.;Chi, Bertie;Thomson, Andrew R.;Boyle, Aimee L.;Bartlett, Gail J.;Bruning, Marc;Linden, Noah;Sessions, Richard B.;Booth, Paula J.;Brady, R. Leo;Woolfson, Derek N.
The design of new proteins that expand the repertoire of natural protein structures represents a formidable challenge. Success in this area would increase understanding of protein structure, and present new scaffolds that could be exploited in biotechnology and synthetic biology. Here we describe the design, characterisation and X-ray crystal structure of a new coiled-coil protein. The de novo sequence forms a stand-alone, parallel, 6-helix bundle with a channel running through it. Although lined exclusively by hydrophobic leucine and isoleucine side chains, the 6 Å channel is permeable to water. One layer of leucine residues within the channel is mutable accepting polar aspartic acid (Asp) and histidine (His) side chains, and leading to subdivision and organization of solvent within the lumen. Moreover, these mutants can be combined to form a stable and unique (Asp-His)3 heterohexamer. These new structures provide a basis for engineering de novo proteins with new functions.
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影响因子:
5.6
作者:
Grigoryan G;Degrado WF
通讯作者:
Degrado WF
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
2.9
作者:
MacDonald, Jarnes T.;Maksimiak, Katarzyna;Taylor, William R.
通讯作者:
Taylor, William R.
影响因子:
64.8
作者:
Grigoryan, Gevorg;Reinke, Aaron W.;Keating, Amy E.
通讯作者:
Keating, Amy E.
DOI:
10.1107/s0907444909052925
发表时间:
2010-02
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
作者:
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者:
Zwart PH