View source for 6tm2


==Human MUC2 AAs 21-1397==
<StructureSection load='6tm2' size='340' side='right'caption='[[6tm2]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6tm2]] is a 6 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=6TM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TM2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.95&#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=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=6tm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tm2 OCA], [https://pdbe.org/6tm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tm2 RCSB], [https://www.ebi.ac.uk/pdbsum/6tm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tm2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MUC2_HUMAN MUC2_HUMAN] Coats the epithelia of the intestines, airways, and other mucus membrane-containing organs. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. Major constituent of both the inner and outer mucus layers of the colon and may play a role in excluding bacteria from the inner mucus layer.<ref>PMID:19432394</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food. Likewise, the vasculature is threatened by inflammation and trauma. Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems. Colon mucins additionally house and feed the gut microbiome. Here, we present an integrated structural analysis of the intestinal mucin MUC2. Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels. Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus. Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2. The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation.

Assembly Mechanism of Mucin and von Willebrand Factor Polymers.,Javitt G, Khmelnitsky L, Albert L, Bigman LS, Elad N, Morgenstern D, Ilani T, Levy Y, Diskin R, Fass D Cell. 2020 Oct 2. pii: S0092-8674(20)31162-4. doi: 10.1016/j.cell.2020.09.021. PMID:33031746<ref>PMID:33031746</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tm2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Albert L]]
[[Category: Diskin R]]
[[Category: Elad N]]
[[Category: Fass D]]
[[Category: Ilani T]]
[[Category: Javitt G]]
[[Category: Khmelnitsky L]]