This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4gwm
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==Crystal structure of human promeprin beta== |
| + | <StructureSection load='4gwm' size='340' side='right' caption='[[4gwm]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4gwm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GWM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GWM FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gwn|4gwn]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MEP1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Meprin_B Meprin B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.63 3.4.24.63] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gwm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gwm RCSB], [http://www.ebi.ac.uk/pdbsum/4gwm PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Meprin B]] | [[Category: Meprin B]] | ||
| - | [[Category: Arolas, J L | + | [[Category: Arolas, J L]] |
| - | [[Category: Becker-Pauly, C | + | [[Category: Becker-Pauly, C]] |
| - | [[Category: Bode, W | + | [[Category: Bode, W]] |
| - | [[Category: Broder, C | + | [[Category: Broder, C]] |
| - | [[Category: Gomis-Ruth, F X | + | [[Category: Gomis-Ruth, F X]] |
| - | [[Category: Guevara, T | + | [[Category: Guevara, T]] |
| - | [[Category: Jefferson, T | + | [[Category: Jefferson, T]] |
| - | [[Category: Sterchi, E E | + | [[Category: Sterchi, E E]] |
| - | [[Category: Stocker, W | + | [[Category: Stocker, W]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Mulidomain structure]] | [[Category: Mulidomain structure]] | ||
Revision as of 09:17, 10 December 2014
Crystal structure of human promeprin beta
| |||||||||||
