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1xof
From Proteopedia
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| - | [[ | + | ==Heterooligomeric Beta Beta Alpha Miniprotein== |
| + | <StructureSection load='1xof' size='340' side='right' caption='[[1xof]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1xof]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XOF FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DBZ:3-(BENZOYLAMINO)-L-ALANINE'>DBZ</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sn9|1sn9]], [[1sna|1sna]], [[1sne|1sne]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xof RCSB], [http://www.ebi.ac.uk/pdbsum/1xof PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:15698566</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Ali, M H.]] | [[Category: Ali, M H.]] | ||
[[Category: Allen, K N.]] | [[Category: Allen, K N.]] | ||
Revision as of 08:23, 8 October 2014
Heterooligomeric Beta Beta Alpha Miniprotein
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