1xof: Difference between revisions

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OCA

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-[[Image:1xof.gif|left|200px]]<br /><applet load="1xof" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1xof, resolution 1.95&Aring;" />
-'''Heterooligomeric Beta Beta Alpha Miniprotein'''<br />
-==Overview==
+==Heterooligomeric Beta Beta Alpha Miniprotein==
-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.
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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.
-==About this Structure==
+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>
-XOF 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XOF OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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]
+</div>
-[[Category: Protein complex]]
+<div class="pdbe-citations 1xof" style="background-color:#fffaf0;"></div>
-[[Category: Ali, M.H.]]
+== References ==
-[[Category: Allen, K.N.]]
+<references/>
-[[Category: Grigoryan, G.]]
+__TOC__
-[[Category: Imperiali, B.]]
+</StructureSection>
-[[Category: Keating, A.E.]]
+[[Category: Large Structures]]
-[[Category: Taylor, C.M.]]
+[[Category: Ali MH]]
-[[Category: ACE]]
+[[Category: Allen KN]]
-[[Category: heterooligomer]]
+[[Category: Grigoryan G]]
-[[Category: heterotetramer]]
+[[Category: Imperiali B]]
-[[Category: protein design]]
+[[Category: Keating AE]]
+[[Category: Taylor CM]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:35:08 2007''