5u66: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Modified single helix from the B-domain of protein A bound to IgG1 Fc== | |||
<StructureSection load='5u66' size='340' side='right' caption='[[5u66]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5u66]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U66 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=85G:N-ETHYL-L-GLUTAMINE'>85G</scene>, <scene name='pdbligand=85J:N-PROPYL-L-GLUTAMINE'>85J</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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=5u66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u66 OCA], [http://pdbe.org/5u66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u66 RCSB], [http://www.ebi.ac.uk/pdbsum/5u66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u66 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. | |||
3-2-1: 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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5u66" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Eigenbrot, C]] | [[Category: Eigenbrot, C]] | ||
[[Category: Ultsch, M H]] | |||
[[Category: B-domain]] | |||
[[Category: Igg1 fc]] | |||
[[Category: Immune system-inhibitor complex]] | |||
[[Category: Protein some]] | |||
[[Category: Staple peptide]] |
Revision as of 16:40, 24 May 2017
Modified single helix from the B-domain of protein A bound to IgG1 FcModified single helix from the B-domain of protein A bound to IgG1 Fc
Structural highlights
Publication Abstract from PubMedThe 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. 3-2-1: 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|