2n7q: Difference between revisions
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==Structure of the transmembrane domain of human nicastrin in SDS micelles== | ==Structure of the transmembrane domain of human nicastrin in SDS micelles== | ||
<StructureSection load='2n7q' size='340' side='right' caption='[[2n7q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2n7q' size='340' side='right'caption='[[2n7q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2n7q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N7Q OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2n7q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N7Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2N7Q FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2n7r|2n7r]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2n7r|2n7r]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2n7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n7q OCA], [http://pdbe.org/2n7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n7q RCSB], [http://www.ebi.ac.uk/pdbsum/2n7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n7q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2n7q" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2n7q" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Gamma secretase complex|Gamma secretase complex]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Kang, C]] | [[Category: Kang, C]] | ||
[[Category: Li, Q]] | [[Category: Li, Q]] | ||
Revision as of 09:31, 20 May 2020
Structure of the transmembrane domain of human nicastrin in SDS micellesStructure of the transmembrane domain of human nicastrin in SDS micelles
Structural highlights
Disease[NICA_HUMAN] Hidradenitis suppurativa. The disease is caused by mutations affecting the gene represented in this entry. Function[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. Publication Abstract from PubMedNicastrin is the largest component of gamma-secretase that is an intramembrane protease important in the development of Alzheimer's disease. Nicastrin contains a large extracellular domain, a single transmembrane (TM) domain, and a short C-terminus. Its TM domain is important for the gamma-secretase complex formation. Here we report nuclear magnetic resonance (NMR) studies of the TM and C-terminal regions of human nicastrin in both sodium dodecyl sulfate (SDS) and dodecylphosphocholine (DPC) micelles. Structural study and dynamic analysis reveal that the TM domain is largely helical and stable under both SDS and DPC micelles with its N-terminal region undergoing intermediate time scale motion. The TM helix contains a hydrophilic patch that is important for TM-TM interactions. The short C-terminus is not structured in solution and a region formed by residues V697-A702 interacts with the membrane, suggesting that these residues may play a role in the gamma-secretase complex formation. Our study provides structural insight into the function of the nicastrin TM domain and the C-terminus in gamma-secretase complex. Structure of the transmembrane domain of human nicastrin-a component of gamma-secretase.,Li Y, Liew LS, Li Q, Kang C Sci Rep. 2016 Jan 18;6:19522. doi: 10.1038/srep19522. PMID:26776682[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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