1xof: Difference between revisions
New page: left|200px<br /><applet load="1xof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xof, resolution 1.95Å" /> '''Heterooligomeric Bet... |
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[[Image:1xof.gif|left|200px]]<br /><applet load="1xof" size=" | [[Image:1xof.gif|left|200px]]<br /><applet load="1xof" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1xof, resolution 1.95Å" /> | caption="1xof, resolution 1.95Å" /> | ||
'''Heterooligomeric Beta Beta Alpha Miniprotein'''<br /> | '''Heterooligomeric Beta Beta Alpha Miniprotein'''<br /> | ||
==Overview== | ==Overview== | ||
The study of short, autonomously folding peptides, or "miniproteins," is | 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. | ||
==About this Structure== | ==About this Structure== | ||
1XOF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1XOF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOF OCA]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15698566 15698566] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15698566 15698566] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ali, M | [[Category: Ali, M H.]] | ||
[[Category: Allen, K | [[Category: Allen, K N.]] | ||
[[Category: Grigoryan, G.]] | [[Category: Grigoryan, G.]] | ||
[[Category: Imperiali, B.]] | [[Category: Imperiali, B.]] | ||
[[Category: Keating, A | [[Category: Keating, A E.]] | ||
[[Category: Taylor, C | [[Category: Taylor, C M.]] | ||
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: heterooligomer]] | [[Category: heterooligomer]] | ||
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[[Category: protein design]] | [[Category: protein design]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:56 2008'' | ||
