View source for 5vgp


==Fc fragment of human IgG1 antibody, from NIST mAb==
<StructureSection load='5vgp' size='340' side='right'caption='[[5vgp]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vgp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VGP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.116&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vgp OCA], [https://pdbe.org/5vgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vgp RCSB], [https://www.ebi.ac.uk/pdbsum/5vgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vgp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6PYX1_HUMAN Q6PYX1_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As the link between antigen binding and immune activation, the antibody Fc region has received extensive structural study. In this report, the structure of the Fc fragment of the NIST IgG1 mAb (reference material 8671) is described at 2.1 A resolution in space group P212121, with approximate unit-cell parameters a = 50, b = 80, c = 138 A. Prior Fc structures with a wide variety of modifications are also surveyed, focusing on those in the same crystal form. To facilitate the analysis of conformations, a reference frame and a two-parameter metric are proposed, considering the CH2 domains as mobile with respect to a fixed dimeric CH3 core. Over several human Fc structures, a significant variation in Fc elbow conformations is observed, which may serve to facilitate the regulation of Fc effector signaling.

Structure of the Fc fragment of the NIST reference antibody RM8671.,Gallagher DT, Galvin CV, Karageorgos I Acta Crystallogr F Struct Biol Commun. 2018 Sep 1;74(Pt 9):524-529. doi:, 10.1107/S2053230X18009834. Epub 2018 Aug 29. PMID:30198883<ref>PMID:30198883</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vgp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Gallagher DT]]
[[Category: Galvin CV]]
[[Category: Karageorgos I]]
[[Category: Marino JP]]