2ls2: Difference between revisions
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< | ==1H Chemical Shift Assignments for the first transmembrane domain from human copper transport 1== | ||
<StructureSection load='2ls2' size='340' side='right'caption='[[2ls2]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ls2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LS2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2ls2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ls2 OCA], [https://pdbe.org/2ls2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ls2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ls2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ls2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/COPT1_HUMAN COPT1_HUMAN] High-affinity, saturable copper transporter involved in dietary copper uptake.<ref>PMID:11734551</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The human copper transporter 1 (hCtr1) mediates cellular uptake of copper and Pt-based chemotherapeutic anticancer drugs. In this paper, we determined the three-dimensional structure and oligomerization of the transmembrane domains (TMDs) of hCtr1 in 40% HFIP aqueous solution by using solution-state NMR spectroscopy. We firstly revealed that TMD1 forms an alpha-helical structure from Gly67 to Glu84 and is dimerized by close packing of its C-terminal helix; TMD2 forms an alpha-helical structure from Leu134 to Thr155 and is self-associated as a trimer by the hydrophobic contact of TMD2 monomers; TMD3 adopts a discontinuous helix structure, known as 'alpha-helix-coiled segment-alpha-helix', and is dimerized by the interaction between the N-terminal helices. The motif GxxxG in TMD3 is not fully involved in the helix, but partially unstructured as a linker between helices. The flexible linker of TMD3 may serve as a gating adapter to mediate pore on and off switch. The differences in the structure and aggregation of the TMD peptides may be related to their different roles in the channel formation and transport function. | |||
Structural insights into the transmembrane domains of human copper transporter 1.,Yang L, Huang Z, Li F J Pept Sci. 2012 Jul;18(7):449-55. doi: 10.1002/psc.2415. Epub 2012 May 21. PMID:22615137<ref>PMID:22615137</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 2ls2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Huang Z]] | ||
[[Category: | [[Category: Li F]] | ||
[[Category: | [[Category: Yang L]] | ||
Latest revision as of 08:50, 15 May 2024
1H Chemical Shift Assignments for the first transmembrane domain from human copper transport 11H Chemical Shift Assignments for the first transmembrane domain from human copper transport 1
Structural highlights
FunctionCOPT1_HUMAN High-affinity, saturable copper transporter involved in dietary copper uptake.[1] Publication Abstract from PubMedThe human copper transporter 1 (hCtr1) mediates cellular uptake of copper and Pt-based chemotherapeutic anticancer drugs. In this paper, we determined the three-dimensional structure and oligomerization of the transmembrane domains (TMDs) of hCtr1 in 40% HFIP aqueous solution by using solution-state NMR spectroscopy. We firstly revealed that TMD1 forms an alpha-helical structure from Gly67 to Glu84 and is dimerized by close packing of its C-terminal helix; TMD2 forms an alpha-helical structure from Leu134 to Thr155 and is self-associated as a trimer by the hydrophobic contact of TMD2 monomers; TMD3 adopts a discontinuous helix structure, known as 'alpha-helix-coiled segment-alpha-helix', and is dimerized by the interaction between the N-terminal helices. The motif GxxxG in TMD3 is not fully involved in the helix, but partially unstructured as a linker between helices. The flexible linker of TMD3 may serve as a gating adapter to mediate pore on and off switch. The differences in the structure and aggregation of the TMD peptides may be related to their different roles in the channel formation and transport function. Structural insights into the transmembrane domains of human copper transporter 1.,Yang L, Huang Z, Li F J Pept Sci. 2012 Jul;18(7):449-55. doi: 10.1002/psc.2415. Epub 2012 May 21. PMID:22615137[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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