5kf4: Difference between revisions

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-'''Unreleased structure'''
-The entry 5kf4 is ON HOLD
+==Crystal structure of FN3 domain (Residues P368-P466) of Human collagen XX==
+<StructureSection load='5kf4' size='340' side='right' caption='[[5kf4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5kf4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KF4 FirstGlance]. <br>
+</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=5kf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kf4 OCA], [http://pdbe.org/5kf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kf4 RCSB], [http://www.ebi.ac.uk/pdbsum/5kf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kf4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/COKA1_HUMAN COKA1_HUMAN]] Probable collagen protein.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The use of consensus design to produce stable proteins has been applied to numerous structures and classes of proteins. Here, we describe the engineering of novel FN3 domains from two different proteins, namely human fibronectin and human tenascin-C, as potential alternative scaffold biotherapeutics. The resulting FN3 domains were found to be robustly expressed in Escherichia coli, soluble and highly stable, with melting temperatures of 89 and 78 degrees C, respectively. X-ray crystallography was used to confirm that the consensus approach led to a structure consistent with the FN3 design despite having only low-sequence identity to natural FN3 domains. The ability of the Tenascin consensus domain to withstand mutations in the loop regions connecting the beta-strands was investigated using alanine scanning mutagenesis demonstrating the potential for randomization in these regions. Finally, rational design was used to produce point mutations that significantly increase the stability of one of the consensus domains. Together our data suggest that consensus FN3 domains have potential utility as alternative scaffold therapeutics.
-Authors: Xie, Y., Cheng, Z., Zhao, J.
+Design of novel FN3 domains with high stability by a consensus sequence approach.,Jacobs SA, Diem MD, Luo J, Teplyakov A, Obmolova G, Malia T, Gilliland GL, O'Neil KT Protein Eng Des Sel. 2012 Mar;25(3):107-17. Epub 2012 Jan 12. PMID:22240293<ref>PMID:22240293</ref>
-Description: Crystal structure of FN3 domain (Residues P368-P466) of Human collagen XX
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5kf4" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Cheng, Z]]
+[[Category: Xie, Y]]
 [[Category: Zhao, J]]
-[[Category: Xie, Y]]
+[[Category: Contractile protein]]
+[[Category: Fn3 domain]]
+[[Category: Human collagen]]