1qys
From Proteopedia
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- | [[ | + | ==Crystal structure of Top7: A computationally designed protein with a novel fold== |
+ | <StructureSection load='1qys' size='340' side='right' caption='[[1qys]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1qys]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Computationally_designed_sequence Computationally designed sequence]. The October 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Designer Proteins'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_10 10.2210/rcsb_pdb/mom_2005_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QYS FirstGlance]. <br> | ||
+ | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1qys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qys OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qys RCSB], [http://www.ebi.ac.uk/pdbsum/1qys PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | A major challenge of computational protein design is the creation of novel proteins with arbitrarily chosen three-dimensional structures. Here, we used a general computational strategy that iterates between sequence design and structure prediction to design a 93-residue alpha/beta protein called Top7 with a novel sequence and topology. Top7 was found experimentally to be folded and extremely stable, and the x-ray crystal structure of Top7 is similar (root mean square deviation equals 1.2 angstroms) to the design model. The ability to design a new protein fold makes possible the exploration of the large regions of the protein universe not yet observed in nature. | ||
- | + | Design of a novel globular protein fold with atomic-level accuracy.,Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, Baker D Science. 2003 Nov 21;302(5649):1364-8. PMID:14631033<ref>PMID:14631033</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Computationally designed sequence]] | [[Category: Computationally designed sequence]] | ||
[[Category: Designer Proteins]] | [[Category: Designer Proteins]] |
Revision as of 08:24, 8 October 2014
Crystal structure of Top7: A computationally designed protein with a novel fold
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