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Structure paper

TitleStructure-function analyses of human TRPV6 ancestral and derived haplotypes.
Journal, issue, pagesStructure, Vol. 33, Issue 1, Page 91-103.e5, Year 2025
Publish dateJan 2, 2025
AuthorsArthur Neuberger / Alexey Shalygin / Yury A Trofimov / Irina I Veretenenko / Kirill D Nadezhdin / Nikolay A Krylov / Thomas Gudermann / Roman G Efremov / Vladimir Chubanov / Alexander I Sobolevsky /
PubMed AbstractTRPV6 is a Ca selective channel that mediates calcium uptake in the gut and contributes to the development and progression of human cancers. TRPV6 is represented by the ancestral and derived ...TRPV6 is a Ca selective channel that mediates calcium uptake in the gut and contributes to the development and progression of human cancers. TRPV6 is represented by the ancestral and derived haplotypes that differ by three non-synonymous polymorphisms, located in the N-terminal ankyrin repeat domain (C157R), S1-S2 extracellular loop (M378V), and C-terminus (M681T). The ancestral and derived haplotypes were proposed to serve as genomic factors causing a different outcome for cancer patients of African ancestry. We solved cryoelectron microscopy (cryo-EM) structures of ancestral and derived TRPV6 in the open and calmodulin (CaM)-bound inactivated states. Neither state shows substantial structural differences caused by the non-synonymous polymorphisms. Functional properties assessed by electrophysiological recordings and Ca uptake measurements, and water and ion permeation evaluated by molecular modeling also appear similar between the haplotypes. Therefore, ancestral and derived TRPV6 have similar structure and function, implying that other factors are responsible for the differences in susceptibility to cancer.
External linksStructure / PubMed:39500315 / PubMed Central
MethodsEM (single particle)
Resolution2.78 - 3.42 Å
Structure data

45933

9cuh

EMDB-45933, PDB-9cuh:
Structure of human full-length ancestral TRPV6 channel in apo open state
Method: EM (single particle) / Resolution: 3.03 Å

45934

9cui

EMDB-45934, PDB-9cui:
Structure of human full-length ancestral TRPV6 channel in Calmodulin-bound state
Method: EM (single particle) / Resolution: 3.42 Å

45935

9cuj

EMDB-45935, PDB-9cuj:
Structure of human full-length derived TRPV6 channel in apo open state
Method: EM (single particle) / Resolution: 2.78 Å

45936

9cuk

EMDB-45936, PDB-9cuk:
Structure of human full-length derived TRPV6 channel in Calmodulin-bound state
Method: EM (single particle) / Resolution: 3.26 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-PCW:
1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipid*YM

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / transient receptor potential V family member 6 / TRP / channel / TRPV6 / TRP channels / ancestral / calmodulin / derived

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