View source for 7rpp


==Crystal structure of human CEACAM1 with GFCC' and ABED face==
<StructureSection load='7rpp' size='340' side='right'caption='[[7rpp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7rpp]] is a 3 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=7RPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RPP 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=7rpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rpp OCA], [https://pdbe.org/7rpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rpp RCSB], [https://www.ebi.ac.uk/pdbsum/7rpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rpp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CEAM1_HUMAN CEAM1_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human (h) CEACAM1 GFCC' face serves as a binding site for homophilic and heterophilic interactions with various microbial and host ligands. hCEACAM1 has also been observed to form oligomers and micro-clusters on the cell surface which are thought to regulate hCEACAM1-mediated signaling. However, the structural basis for hCEACAM1 higher-order oligomerization is currently unknown. To understand this, we report a hCEACAM1 IgV oligomer crystal structure which shows how GFCC' face-mediated homodimerization enables highly flexible ABED face interactions to arise. Structural modeling and nuclear magnetic resonance (NMR) studies predict that such oligomerization is not impeded by the presence of carbohydrate side-chain modifications. In addition, using UV spectroscopy and NMR studies, we show that oligomerization is further facilitated by the presence of a conserved metal ion (Zn(++) or Ni(++)) binding site on the G strand of the FG loop. Together these studies provide biophysical insights on how GFCC' and ABED face interactions together with metal ion binding may facilitate hCEACAM1 oligomerization beyond dimerization.

Structural analysis of human CEACAM1 oligomerization.,Gandhi AK, Sun ZJ, Huang YH, Kim WM, Yang C, Petsko GA, Beauchemin N, Blumberg RS Commun Biol. 2022 Sep 30;5(1):1042. doi: 10.1038/s42003-022-03996-4. PMID:36180783<ref>PMID:36180783</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7rpp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Blumberg RS]]
[[Category: Gandhi AK]]
[[Category: Huang YH]]
[[Category: Kim WM]]
[[Category: Petsko GA]]
[[Category: Sun Z-Y]]