2RFA

Crystal structure of the mouse TRPV6 ankyrin repeat domain

Summary for 2RFA

• Entry DOI: 10.2210/pdb2rfa/pdb
• Descriptor: Transient receptor potential cation channel subfamily V member 6 (2 entities in total)
• Functional Keywords: trpv6, ankyrin reapeat, transient receptor potential, ank repeat, calcium channel, calcium transport, calmodulin-binding, glycoprotein, ion transport, ionic channel, membrane, transmembrane, transport, membrane protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane ; Multi- pass membrane protein : Q91WD2
• Total number of polymer chains: 1
• Total formula weight: 25707.59

Authors

Phelps, C.B.,Huang, R.J.,Wang, R.R.,Gaudet, R. (deposition date: 2007-09-28, release date: 2008-02-19, Last modification date: 2024-02-21)

Primary citation

Phelps, C.B.,Huang, R.J.,Lishko, P.V.,Wang, R.R.,Gaudet, R.
Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels.
Biochemistry, 47:2476-2484, 2008

PubMed Abstract: Transient receptor potential (TRP) proteins are cation channels composed of a transmembrane domain flanked by large N- and C-terminal cytoplasmic domains. All members of the vanilloid family of TRP channels (TRPV) possess an N-terminal ankyrin repeat domain (ARD). The ARD of mammalian TRPV6, an important regulator of calcium uptake and homeostasis, is essential for channel assembly and regulation. The 1.7 A crystal structure of the TRPV6-ARD reveals conserved structural elements unique to the ARDs of TRPV proteins. First, a large twist between the fourth and fifth repeats is induced by residues conserved in all TRPV ARDs. Second, the third finger loop is the most variable region in sequence, length and conformation. In TRPV6, a number of putative regulatory phosphorylation sites map to the base of this third finger. Size exclusion chromatography and crystal packing indicate that the TRPV6-ARD does not assemble as a tetramer and is monomeric in solution. Adenosine triphosphate-agarose and calmodulin-agarose pull-down assays show that the TRPV6-ARD does not interact with either ligand, indicating a different functional role for the TRPV6-ARD than in the paralogous thermosensitive TRPV1 channel. Similar biochemical findings are also presented for the highly homologous mammalian TRPV5-ARD. The implications of the structural and biochemical data on the role of the ankyrin repeats in different TRPV channels are discussed.

PubMed: 18232717
DOI: 10.1021/bi702109w

Experimental method

X-RAY DIFFRACTION (1.7 Å)