7mu8
From Proteopedia
(Difference between revisions)
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==Structure of the minimally glycosylated human CEACAM1 N-terminal domain== | ==Structure of the minimally glycosylated human CEACAM1 N-terminal domain== | ||
| - | <StructureSection load='7mu8' size='340' side='right'caption='[[7mu8]]' scene=''> | + | <StructureSection load='7mu8' size='340' side='right'caption='[[7mu8]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MU8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7mu8]] 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=7MU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MU8 FirstGlance]. <br> |
| - | </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=7mu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mu8 OCA], [https://pdbe.org/7mu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mu8 RCSB], [https://www.ebi.ac.uk/pdbsum/7mu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mu8 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7mu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mu8 OCA], [https://pdbe.org/7mu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mu8 RCSB], [https://www.ebi.ac.uk/pdbsum/7mu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mu8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CEAM1_HUMAN CEAM1_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Carcinoembryonic cellular adhesion molecules (CEACAMs) serve diverse roles in cell signaling, proliferation, and survival and are made up of one or several immunoglobulin (Ig)-like ectodomains glycosylated in vivo. The physiological oligomeric state and how it contributes to protein function are central to understanding CEACAMs. Two putative dimer conformations involving different CEACAM1 N-terminal Ig-like domain (CCM1) protein faces (ABED and GFCC'C'') were identified from crystal structures. GFCC'C'' was identified as the dominant CCM1 solution dimer, but ambiguity regarding the effect of glycosylation on dimer formation calls its physiological relevance into question. We present the first crystal structure of minimally glycosylated CCM1 in the GFCC'C'' dimer conformation and characterization in solution by continuous-wave and double electron-electron resonance electron paramagnetic resonance spectroscopy. Our results suggest the GFCC'C'' dimer is dominant in solution with different levels of glycosylation, and structural conservation and co-evolved residues support that the GFCC'C'' dimer is conserved across CEACAMs. | ||
| + | |||
| + | Human CEACAM1 N-domain dimerization is independent from glycan modifications.,Belcher Dufrisne M, Swope N, Kieber M, Yang JY, Han J, Li J, Moremen KW, Prestegard JH, Columbus L Structure. 2022 May 5;30(5):658-670.e5. doi: 10.1016/j.str.2022.02.003. Epub 2022, Feb 25. PMID:35219398<ref>PMID:35219398</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7mu8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Belcher Dufrisne M]] | [[Category: Belcher Dufrisne M]] | ||
Revision as of 16:20, 18 October 2023
Structure of the minimally glycosylated human CEACAM1 N-terminal domain
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Categories: Homo sapiens | Large Structures | Belcher Dufrisne M | Columbus L | Han J | Kieber M | Li J | Moremen KW | Prestegard JH | Swope N | Yang JY
