5u52: Difference between revisions

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-'''Unreleased structure'''
-The entry 5u52 is ON HOLD  until Paper Publication
+==2 helix minimized version of the B-domain from Protein A (Z34C0 bound to IgG1 Fc (monoclinic form)==
+<StructureSection load='5u52' size='340' side='right' caption='[[5u52]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5u52]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U52 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l6x|1l6x]], [[5u4y|5u4y]], [[5u66|5u66]]</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=5u52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u52 OCA], [http://pdbe.org/5u52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u52 RCSB], [http://www.ebi.ac.uk/pdbsum/5u52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u52 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The well-studied B-domain from Staphylococcal protein A is a 59 amino acid three-helix bundle that binds the Fc portion of IgG with a dissociation constant of ~35 nM. The B-domain variant bearing a Gly to Ala mutation (=Z-domain) has been the subject of efforts to minimize a domain's size while retaining its function. We report X-ray crystallographic characterization of three steps in such a process using complexes with Fc: the full three-helix Z-domain, a 34 amino acid two-helix version called Z34C and a 13 amino acid single helix stabilized with an exo-helix tether, called LH1.
-Authors:
+-2-1: Structural insights from stepwise shrinkage of a three-helix Fc-binding domain to a single helix.,Ultsch M, Braisted A, Maun HR, Eigenbrot C Protein Eng Des Sel. 2017 May 5:1-7. doi: 10.1093/protein/gzx029. PMID:28475752<ref>PMID:28475752</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5u52" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Eigenbrot, C]]
+[[Category: Ultsch, M H]]
+[[Category: Helix bundle]]
+[[Category: B-domain]]
+[[Category: Igg1 fc]]
+[[Category: Immune system]]
+[[Category: Protein some]]