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Structural insights into the transmembrane domains of human copper transporter 1.

Yang L, Huang Z, Li F
J Pept Sci 18 449-55 (2012)
Related entries: 2ls2, 2ls3

Cited: 3 times
EuropePMC logo PMID: 22615137

Abstract

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 α-helical structure from Gly67 to Glu84 and is dimerized by close packing of its C-terminal helix; TMD2 forms an α-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 'α-helix-coiled segment-α-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.

Articles - 2ls4 mentioned but not cited (1)

  1. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)


Articles citing this publication (2)

  1. How copper traverses cellular membranes through the mammalian copper transporter 1, Ctr1. Ohrvik H, Thiele DJ. Ann. N. Y. Acad. Sci. 1314 32-41 (2014)
  2. Cu(i) and Ag(i) complex formation with the hydrophilic phosphine 1,3,5-triaza-7-phosphadamantane in different ionic media. How to estimate the effect of a complexing medium. Endrizzi F, Di Bernardo P, Zanonato PL, Tisato F, Porchia M, Ahmed Isse A, Melchior A, Tolazzi M. Dalton Trans 46 1455-1466 (2017)


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