5u66: Difference between revisions

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'''Unreleased structure'''


The entry 5u66 is ON HOLD  until Paper Publication
==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]] 1.70&Aring;' 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.


Authors: Ultsch, M.H., Eigenbrot, C.
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>


Description: Modified single helix from the B-domain of protein A bound to IgG1 Fc
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Ultsch, M.H]]
<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

5u66 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Ultsch M, Braisted A, Maun HR, Eigenbrot C. 3-2-1: Structural insights from stepwise shrinkage of a three-helix Fc-binding domain to a single helix. Protein Eng Des Sel. 2017 May 5:1-7. doi: 10.1093/protein/gzx029. PMID:28475752 doi:http://dx.doi.org/10.1093/protein/gzx029

5u66, resolution 1.70Å

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