4gwn: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: '''Unreleased structure''' The entry 4gwn is ON HOLD Authors: Arolas, J.L., Broder, C., Jefferson, T., Guevara, T., Sterchi, E.E., Bode, W., Stocker, W., Becker-Pauly, C., Gomis-Ruth, F...
 
OCA (talk | contribs)
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4gwn is ON HOLD
==Crystal structure of human mature meprin beta==
<StructureSection load='4gwn' size='340' side='right'caption='[[4gwn]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4gwn]] 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=4GWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GWN 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]] 3&#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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4gwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gwn OCA], [https://pdbe.org/4gwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gwn RCSB], [https://www.ebi.ac.uk/pdbsum/4gwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gwn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MEP1B_HUMAN MEP1B_HUMAN] Membrane metallopeptidase that sheds many membrane-bound proteins. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components.<ref>PMID:21693781</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane. Human meprin beta is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression. In addition, it cleaves amyloid precursor protein (APP) at the beta-secretase site, giving rise to amyloidogenic peptides. We have solved the X-ray crystal structure of a major fragment of the meprin beta ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen. The meprin beta dimer displays a compact shape, whose catalytic domain undergoes major rearrangement upon activation, and reveals an exosite and a sugar-rich channel, both of which possibly engage in substrate binding. A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.


Authors: Arolas, J.L., Broder, C., Jefferson, T., Guevara, T., Sterchi, E.E., Bode, W., Stocker, W., Becker-Pauly, C., Gomis-Ruth, F.X.
Structural basis for the sheddase function of human meprin beta metalloproteinase at the plasma membrane.,Arolas JL, Broder C, Jefferson T, Guevara T, Sterchi EE, Bode W, Stocker W, Becker-Pauly C, Gomis-Ruth FX Proc Natl Acad Sci U S A. 2012 Oct 2;109(40):16131-6. doi:, 10.1073/pnas.1211076109. Epub 2012 Sep 17. PMID:22988105<ref>PMID:22988105</ref>


Description: Crystal structure of human mature meprin beta
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4gwn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arolas JL]]
[[Category: Becker-Pauly C]]
[[Category: Bode W]]
[[Category: Broder C]]
[[Category: Gomis-Ruth FX]]
[[Category: Guevara T]]
[[Category: Jefferson T]]
[[Category: Sterchi EE]]
[[Category: Stocker W]]