View source for 1xof


==Heterooligomeric Beta Beta Alpha Miniprotein==
<StructureSection load='1xof' size='340' side='right'caption='[[1xof]], [[Resolution|resolution]] 1.95&Aring;' 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 [https://proteopedia.org/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"><div style='overflow: auto; max-height: 3em;'>[[1sn9|1sn9]], [[1sna|1sna]], [[1sne|1sne]]</div></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xof OCA], [https://pdbe.org/1xof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xof RCSB], [https://www.ebi.ac.uk/pdbsum/1xof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xof ProSAT]</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1xof" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ali, M H]]
[[Category: Allen, K N]]
[[Category: Grigoryan, G]]
[[Category: Imperiali, B]]
[[Category: Keating, A E]]
[[Category: Taylor, C M]]
[[Category: De novo protein]]
[[Category: Heterooligomer]]
[[Category: Heterotetramer]]
[[Category: Protein design]]