View source for 6chf


==Crystal structure of a Fc fragment LALA mutant (L234A, L235A) of human IgG1 (crystal form 1)==
<StructureSection load='6chf' size='340' side='right'caption='[[6chf]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6chf]] 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=6CHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CHF 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]] 2.4&#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=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=6chf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6chf OCA], [https://pdbe.org/6chf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6chf RCSB], [https://www.ebi.ac.uk/pdbsum/6chf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6chf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6MZV7_HUMAN Q6MZV7_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antibody structure couples adaptive and innate immunity via Fab (antigen binding) and Fc (effector) domains that are connected by unique hinge regions. Because antibodies harbor two or more Fab domains, they are capable of crosslinking multi-determinant antigens, which is required for Fc-dependent functions through associative interactions with effector ligands, including C1q and cell surface Fc receptors. The modular nature of antibodies, with distal ligand binding sites for antigen and Fc-ligands, is reminiscent of allosteric proteins, suggesting that allosteric interactions might contribute to Fc-mediated effector functions. This hypothesis has been pursued for over 40 years and remains unresolved. Here, we provide evidence that allosteric interactions between Fab and Fc triggered by antigen binding modulate binding of Fc to low-affinity Fc receptors (FcgammaR) for a human IgG1. This work opens the path to further dissection of the relative roles of allosteric and associative interactions in Fc-mediated effector functions.

Antigen-Induced Allosteric Changes in a Human IgG1 Fc Increase Low-Affinity Fcgamma Receptor Binding.,Orlandi C, Deredge D, Ray K, Gohain N, Tolbert W, DeVico AL, Wintrode P, Pazgier M, Lewis GK Structure. 2020 May 5;28(5):516-527.e5. doi: 10.1016/j.str.2020.03.001. Epub 2020, Mar 24. PMID:32209433<ref>PMID:32209433</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6chf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Gohain N]]
[[Category: Pazgier M]]
[[Category: Tolbert WD]]