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| - | | + | #REDIRECT [[5a63]] This PDB entry is obsolete and replaced by 5a63 |
| - | ==Structure of a extracellular domain==
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| - | <StructureSection load='4upc' size='340' side='right' caption='[[4upc]], [[Resolution|resolution]] 5.40Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4upc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UPC FirstGlance]. <br>
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| - | </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=4upc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upc OCA], [http://pdbe.org/4upc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4upc RCSB], [http://www.ebi.ac.uk/pdbsum/4upc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4upc ProSAT]</span></td></tr>
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| - | </table>
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| - | == Disease ==
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| - | [[http://www.uniprot.org/uniprot/NICA_HUMAN NICA_HUMAN]] Hidradenitis suppurativa. The disease is caused by mutations affecting the gene represented in this entry.
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/NICA_HUMAN NICA_HUMAN]] Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). It probably represents a stabilizing cofactor required for the assembly of the gamma-secretase complex.
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The gamma-secretase complex, comprising presenilin 1 (PS1), PEN-2, APH-1 and nicastrin, is a membrane-embedded protease that controls a number of important cellular functions through substrate cleavage. Aberrant cleavage of the amyloid precursor protein (APP) results in aggregation of amyloid-beta, which accumulates in the brain and consequently causes Alzheimer's disease. Here we report the three-dimensional structure of an intact human gamma-secretase complex at 4.5 A resolution, determined by cryo-electron-microscopy single-particle analysis. The gamma-secretase complex comprises a horseshoe-shaped transmembrane domain, which contains 19 transmembrane segments (TMs), and a large extracellular domain (ECD) from nicastrin, which sits immediately above the hollow space formed by the TM horseshoe. Intriguingly, nicastrin ECD is structurally similar to a large family of peptidases exemplified by the glutamate carboxypeptidase PSMA. This structure serves as an important basis for understanding the functional mechanisms of the gamma-secretase complex.
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| - | Three-dimensional structure of human gamma-secretase.,Lu P, Bai XC, Ma D, Xie T, Yan C, Sun L, Yang G, Zhao Y, Zhou R, Scheres SH, Shi Y Nature. 2014 Jun 29. doi: 10.1038/nature13567. PMID:25043039<ref>PMID:25043039</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4upc" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Bai, X C]]
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| - | [[Category: Lu, P]]
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| - | [[Category: Ma, D]]
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| - | [[Category: Scheres, S H.W]]
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| - | [[Category: Shi, Y]]
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| - | [[Category: Sun, L]]
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| - | [[Category: Xie, T]]
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| - | [[Category: Yan, C]]
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| - | [[Category: Yang, G]]
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| - | [[Category: Zhao, Y]]
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| - | [[Category: Zhou, R]]
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| - | [[Category: Protein binding]]
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