1xof: Difference between revisions
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== Structural highlights == | == 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> | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</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> | <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> | </table> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ali | [[Category: Ali MH]] | ||
[[Category: Allen | [[Category: Allen KN]] | ||
[[Category: Grigoryan | [[Category: Grigoryan G]] | ||
[[Category: Imperiali | [[Category: Imperiali B]] | ||
[[Category: Keating | [[Category: Keating AE]] | ||
[[Category: Taylor | [[Category: Taylor CM]] | ||
Latest revision as of 10:52, 12 July 2023
Heterooligomeric Beta Beta Alpha MiniproteinHeterooligomeric Beta Beta Alpha Miniprotein
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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