View source for 8ov0


==MUC5AC CysD7 amino acids 3518-3626==
<StructureSection load='8ov0' size='340' side='right'caption='[[8ov0]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ov0]] is a 1 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=8OV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OV0 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=8ov0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ov0 OCA], [https://pdbe.org/8ov0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ov0 RCSB], [https://www.ebi.ac.uk/pdbsum/8ov0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ov0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MUC5A_HUMAN MUC5A_HUMAN] Gel-forming glycoprotein of gastric and respiratory tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microorganisms and particles that are subsequently removed by the mucociliary system (PubMed:14535999, PubMed:14718370). Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD) (PubMed:14535999).<ref>PMID:14535999</ref> <ref>PMID:14535999</ref> <ref>PMID:14718370</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CysD domains are disulfide-rich modules embedded within long O-glycosylated regions of mucin glycoproteins. CysD domains are thought to mediate intermolecular adhesion during the intracellular bioassembly of mucin polymers and perhaps also after secretion in extracellular mucus hydrogels. The human genome encodes 18 CysD domains distributed across three different mucins. To date, experimental structural information is available only for the first CysD domain (CysD1) of the intestinal mucin MUC2, which is one of the most divergent of the CysDs. To provide experimental data on a CysD that is representative of a larger branch of the fold family, we determined the crystal structure of the seventh CysD domain (CysD7) from MUC5AC, a mucin found in the respiratory tract and stomach. The MUC5AC CysD7 structure revealed a single calcium-binding site, contrasting with the two sites in MUC2 CysD1. The MUC5AC CysD7 structure also contained an additional alpha-helix absent from MUC2 CysD1, with potential functional implications for intermolecular interactions. Lastly, the experimental structure emphasized the flexibility of the loop analogous to the main adhesion loop of MUC2 CysD1, suggesting that both sequence divergence and physical plasticity in this region may contribute to the adaptation of mucin CysD domains.

Diversity of CysD domains in gel-forming mucins.,Khmelnitsky L, Milo A, Dym O, Fass D FEBS J. 2023 Aug 1. doi: 10.1111/febs.16918. PMID:37526947<ref>PMID:37526947</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ov0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Dym O]]
[[Category: Fass D]]
[[Category: Khmelnitsky L]]
[[Category: Milo A]]