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PDBsum entry 2f37
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protein ligands Protein-protein interface(s) links
Membrane protein PDB id
2f37

 

 

 

 

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Contents
Protein chain
247 a.a. *
Ligands
SO4 ×2
Waters ×389
* Residue conservation analysis
PDB id:
2f37
Name: Membrane protein
Title: Crystal structure of the ankyrin repeat domain of human trpv2
Structure: Transient receptor potential cation channel subfamily v member 2. Chain: a, b. Fragment: ankyrin repeat domain (residues 69-319). Synonym: trpv2, osm-9-like trp channel 2, otrpc2, vanilloid receptor- like protein 1, vrl-1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: trpv2, vrl. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.208     R-free:   0.229
Authors: C.J.Mccleverty
Key ref:
C.J.McCleverty et al. (2006). Crystal structure of the human TRPV2 channel ankyrin repeat domain. Protein Sci, 15, 2201-2206. PubMed id: 16882997 DOI: 10.1110/ps.062357206
Date:
18-Nov-05     Release date:   31-Oct-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9Y5S1  (TRPV2_HUMAN) -  Transient receptor potential cation channel subfamily V member 2 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		764 a.a.
247 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1110/ps.062357206 Protein Sci 15:2201-2206 (2006)
PubMed id: 16882997  
 
 
Crystal structure of the human TRPV2 channel ankyrin repeat domain.
C.J.McCleverty, E.Koesema, A.Patapoutian, S.A.Lesley, A.Kreusch.
 
  ABSTRACT  
 
TRPV channels are important polymodal integrators of noxious stimuli mediating thermosensation and nociception. An ankyrin repeat domain (ARD), which is a common protein-protein recognition domain, is conserved in the N-terminal intracellular domain of all TRPV channels and predicted to contain three to four ankyrin repeats. Here we report the first structure from the TRPV channel subfamily, a 1.7 A resolution crystal structure of the human TRPV2 ARD. Our crystal structure reveals a six ankyrin repeat stack with multiple insertions in each repeat generating several unique features compared with a canonical ARD. The surface typically used for ligand recognition, the ankyrin groove, contains extended loops with an exposed hydrophobic patch and a prominent kink resulting from a large rotational shift of the last two repeats. The TRPV2 ARD provides the first structural insight into a domain that coordinates nociceptive sensory transduction and is likely to be a prototype for other TRPV channel ARDs.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Ankyrin repeat domain (ARD) of human TRPV2. (A) Stereo ribbon representation of the human TRPV2 ARD superposed
 
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2006, 15, 2201-2206) copyright 2006.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19864432 C.B.Phelps, R.R.Wang, S.S.Choo, and R.Gaudet (2010).
Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain.
  J Biol Chem, 285, 731-740.  
20044482 H.Shigematsu, T.Sokabe, R.Danev, M.Tominaga, and K.Nagayama (2010).
A 3.5-nm structure of rat TRPV4 cation channel revealed by Zernike phase-contrast cryoelectron microscopy.
  J Biol Chem, 285, 11210-11218.  
20037588 M.Auer-Grumbach, A.Olschewski, L.Papić, H.Kremer, M.E.McEntagart, S.Uhrig, C.Fischer, E.Fröhlich, Z.Bálint, B.Tang, H.Strohmaier, H.Lochmüller, B.Schlotter-Weigel, J.Senderek, A.Krebs, K.J.Dick, R.Petty, C.Longman, N.E.Anderson, G.W.Padberg, H.J.Schelhaas, C.M.van Ravenswaaij-Arts, T.R.Pieber, A.H.Crosby, and C.Guelly (2010).
Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C.
  Nat Genet, 42, 160-164.  
21203922 W.Cheng, C.Sun, and J.Zheng (2010).
Heteromerization of TRP channel subunits: extending functional diversity.
  Protein Cell, 1, 802-810.  
19561608 H.Salazar, A.Jara-Oseguera, E.Hernández-García, I.Llorente, I.I.Arias-Olguín, M.Soriano-García, L.D.Islas, and T.Rosenbaum (2009).
Structural determinants of gating in the TRPV1 channel.
  Nat Struct Mol Biol, 16, 704-710.  
  19237587 R.Gaudet (2009).
Divide and conquer: high resolution structural information on TRP channel fragments.
  J Gen Physiol, 133, 231-237.  
20025796 R.Latorre, C.Zaelzer, and S.Brauchi (2009).
Structure-functional intimacies of transient receptor potential channels.
  Q Rev Biophys, 42, 201-246.  
  19237588 V.Y.Moiseenkova-Bell, and T.G.Wensel (2009).
Hot on the trail of TRP channel structure.
  J Gen Physiol, 133, 239-244.  
18232717 C.B.Phelps, R.J.Huang, P.V.Lishko, R.R.Wang, and R.Gaudet (2008).
Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels.
  Biochemistry, 47, 2476-2484.
PDB code: 2rfa
18414734 R.Gaudet (2008).
A primer on ankyrin repeat function in TRP channels and beyond.
  Mol Biosyst, 4, 372-379.  
18490661 V.Y.Moiseenkova-Bell, L.A.Stanciu, I.I.Serysheva, B.J.Tobe, and T.G.Wensel (2008).
Structure of TRPV1 channel revealed by electron cryomicroscopy.
  Proc Natl Acad Sci U S A, 105, 7451-7455.  
17521566 D.L.Minor (2007).
The neurobiologist's guide to structural biology: a primer on why macromolecular structure matters and how to evaluate structural data.
  Neuron, 54, 511-533.  
17706410 M.Bandell, L.J.Macpherson, and A.Patapoutian (2007).
From chills to chilis: mechanisms for thermosensation and chemesthesis via thermoTRPs.
  Curr Opin Neurobiol, 17, 490-497.  
  17325193 W.Cheng, F.Yang, C.L.Takanishi, and J.Zheng (2007).
Thermosensitive TRPV channel subunits coassemble into heteromeric channels with intermediate conductance and gating properties.
  J Gen Physiol, 129, 191-207.  
17065148 I.Erler, D.M.Al-Ansary, U.Wissenbach, T.F.Wagner, V.Flockerzi, and B.A.Niemeyer (2006).
Trafficking and assembly of the cold-sensitive TRPM8 channel.
  J Biol Chem, 281, 38396-38404.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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