1hcw
From Proteopedia
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[[Image:1hcw.gif|left|200px]] | [[Image:1hcw.gif|left|200px]] | ||
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'''23-RESIDUE DESIGNED METAL-FREE PEPTIDE BASED ON THE ZINC FINGER DOMAINS, NMR, 35 STRUCTURES''' | '''23-RESIDUE DESIGNED METAL-FREE PEPTIDE BASED ON THE ZINC FINGER DOMAINS, NMR, 35 STRUCTURES''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCW OCA]. | |
==Reference== | ==Reference== | ||
Design of a monomeric 23-residue polypeptide with defined tertiary structure., Struthers MD, Cheng RP, Imperiali B, Science. 1996 Jan 19;271(5247):342-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8553067 8553067] | Design of a monomeric 23-residue polypeptide with defined tertiary structure., Struthers MD, Cheng RP, Imperiali B, Science. 1996 Jan 19;271(5247):342-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8553067 8553067] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Cheng, R P.]] | [[Category: Cheng, R P.]] | ||
[[Category: Imperiali, B.]] | [[Category: Imperiali, B.]] | ||
[[Category: Struthers, M.]] | [[Category: Struthers, M.]] | ||
| - | [[Category: | + | [[Category: De novo protein design]] |
| - | [[Category: | + | [[Category: Growth response protein]] |
| - | [[Category: | + | [[Category: Supersecondary motif]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:42:43 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:42, 2 May 2008
23-RESIDUE DESIGNED METAL-FREE PEPTIDE BASED ON THE ZINC FINGER DOMAINS, NMR, 35 STRUCTURES
Overview
Small proteins or protein domains generally require disulfide bridges or metal sites for their stabilization. Here it is shown that the beta beta alpha architecture of zinc fingers can be reproduced in a 23-residue polypeptide in the absence of metal ions. The sequence was obtained through an iterative design process. A key feature of the final design is the incorporation of a type II' beta turn to aid in beta-hairpin formation. Nuclear magnetic resonance analysis reveals that the alpha helix and beta hairpin are held together by a defined hydrophobic core. The availability of this structural template has implications for the development of functional polypeptides.
About this Structure
Full crystallographic information is available from OCA.
Reference
Design of a monomeric 23-residue polypeptide with defined tertiary structure., Struthers MD, Cheng RP, Imperiali B, Science. 1996 Jan 19;271(5247):342-5. PMID:8553067 Page seeded by OCA on Fri May 2 18:42:43 2008
