1xof

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{{STRUCTURE_1xof| PDB=1xof | SCENE= }}
{{STRUCTURE_1xof| PDB=1xof | SCENE= }}
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'''Heterooligomeric Beta Beta Alpha Miniprotein'''
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===Heterooligomeric Beta Beta Alpha Miniprotein===
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==Overview==
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The study of short, autonomously folding peptides, or "miniproteins," is important for advancing our understanding of protein stability and folding specificity. Although many examples of synthetic alpha-helical structures are known, relatively few mixed alpha/beta structures have been successfully designed. Only one mixed-secondary structure oligomer, an alpha/beta homotetramer, has been reported thus far. In this report, we use structural analysis and computational design to convert this homotetramer into the smallest known alpha/beta-heterotetramer. Computational screening of many possible sequence/structure combinations led efficiently to the design of short, 21-residue peptides that fold cooperatively and autonomously into a specific complex in solution. A 1.95 A crystal structure reveals how steric complementarity and charge patterning encode heterospecificity. The first- and second-generation heterotetrameric miniproteins described here will be useful as simple models for the analysis of protein-protein interaction specificity and as structural platforms for the further elaboration of folding and function.
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{{ABSTRACT_PUBMED_15698566}}
==About this Structure==
==About this Structure==
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[[Category: Heterotetramer]]
[[Category: Heterotetramer]]
[[Category: Protein design]]
[[Category: Protein design]]
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Revision as of 12:20, 29 July 2008

Image:1xof.png

Template:STRUCTURE 1xof

Heterooligomeric Beta Beta Alpha Miniprotein

Template:ABSTRACT PUBMED 15698566

About this Structure

Full crystallographic information is available from OCA.

Reference

Design of a heterospecific, tetrameric, 21-residue miniprotein with mixed alpha/beta structure., Ali MH, Taylor CM, Grigoryan G, Allen KN, Imperiali B, Keating AE, Structure. 2005 Feb;13(2):225-34. PMID:15698566

Page seeded by OCA on Tue Jul 29 15:20:27 2008

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