6be6

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==ADAM10 Extracellular Domain==
==ADAM10 Extracellular Domain==
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<StructureSection load='6be6' size='340' side='right' caption='[[6be6]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='6be6' size='340' side='right'caption='[[6be6]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6be6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BE6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6be6]] is a 4 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=6BE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BE6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6bdz|6bdz]]</td></tr>
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<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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ADAM10_endopeptidase ADAM10 endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.81 3.4.24.81] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6be6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6be6 OCA], [https://pdbe.org/6be6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6be6 RCSB], [https://www.ebi.ac.uk/pdbsum/6be6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6be6 ProSAT]</span></td></tr>
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<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=6be6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6be6 OCA], [http://pdbe.org/6be6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6be6 RCSB], [http://www.ebi.ac.uk/pdbsum/6be6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6be6 ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/ADA10_HUMAN ADA10_HUMAN]] Reticulate acropigmentation of Kitamura. The disease is caused by mutations affecting the gene represented in this entry. Disease susceptibility is associated with variations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/ADA10_HUMAN ADA10_HUMAN] Reticulate acropigmentation of Kitamura. The disease is caused by mutations affecting the gene represented in this entry. Disease susceptibility is associated with variations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ADA10_HUMAN ADA10_HUMAN]] Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:26686862, PubMed:11786905). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146).[UniProtKB:O35598]<ref>PMID:11477090</ref> <ref>PMID:11786905</ref> <ref>PMID:12475894</ref> <ref>PMID:16239146</ref> <ref>PMID:17557115</ref> <ref>PMID:19114711</ref> <ref>PMID:20592283</ref> <ref>PMID:21288900</ref> <ref>PMID:26686862</ref>
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[https://www.uniprot.org/uniprot/ADA10_HUMAN ADA10_HUMAN] Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:26686862, PubMed:11786905). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146).[UniProtKB:O35598]<ref>PMID:11477090</ref> <ref>PMID:11786905</ref> <ref>PMID:12475894</ref> <ref>PMID:16239146</ref> <ref>PMID:17557115</ref> <ref>PMID:19114711</ref> <ref>PMID:20592283</ref> <ref>PMID:21288900</ref> <ref>PMID:26686862</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6be6" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6be6" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[A Disintegrin And Metalloproteinase 3D structures|A Disintegrin And Metalloproteinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: ADAM10 endopeptidase]]
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[[Category: Homo sapiens]]
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[[Category: Seegar, T C.M]]
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[[Category: Large Structures]]
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[[Category: Adam10]]
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[[Category: Seegar TCM]]
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[[Category: Membrane protein]]
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Current revision

ADAM10 Extracellular Domain

PDB ID 6be6

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