1xof: Difference between revisions

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{{Seed}}
[[Image:1xof.png|left|200px]]


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==Heterooligomeric Beta Beta Alpha Miniprotein==
The line below this paragraph, containing "STRUCTURE_1xof", creates the "Structure Box" on the page.
<StructureSection load='1xof' size='340' side='right'caption='[[1xof]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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<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>
{{STRUCTURE_1xof|  PDB=1xof  |  SCENE= }}
<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.


===Heterooligomeric Beta Beta Alpha Miniprotein===
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>
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(as it appears on PubMed at http://www.pubmed.gov), where 15698566 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15698566}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOF OCA].
[[Category: Ali MH]]
 
[[Category: Allen KN]]
==Reference==
[[Category: Grigoryan G]]
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://www.ncbi.nlm.nih.gov/pubmed/15698566 15698566]
[[Category: Imperiali B]]
[[Category: Ali, M H.]]
[[Category: Keating AE]]
[[Category: Allen, K N.]]
[[Category: Taylor CM]]
[[Category: Grigoryan, G.]]
[[Category: Imperiali, B.]]
[[Category: Keating, A E.]]
[[Category: Taylor, C M.]]
[[Category: Heterooligomer]]
[[Category: Heterotetramer]]
[[Category: Protein design]]
 
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