Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin

被引：25

作者：

Grycova, Lenka ^{[1
]}

Lansky, Zdenek ^{[1
]}

Friedlova, Eliska ^{[1
]}

Obsilova, Veronika ^{[1
]}

Janouskova, Hana ^{[1
]}

Obsil, Tomas ^{[1
,2
]}

Teisinger, Jan ^{[1
]}

机构：

[1] Acad Sci Czech Republic, Inst Physiol, CR-14220 Prague, Czech Republic

[2] Charles Univ Prague, Fac Sci, Dept Phys & Macromol Chem, Prague 12843, Czech Republic

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 375卷 / 04期

关键词：

Vanilloid receptor; TRPV1; Calmodulin; Fluorescence anisotropy;

D O I：

10.1016/j.bbrc.2008.08.094

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calmodulin (CaM) is known to play an important role in the regulation of TRP channels activity. Although it has been reported that CaM binds to the C-terminus of TRPV1 (TRPV1-CT), no classic CaM-binding motif was found in this region. In this work, we explored this unusual TRPV1 CaM-binding motif in detail and found that five residues from a putative CaM-binding motif are important for TRPV1-CT's binding to CaM, with arginine R785 being the most essential residue. The homology modelling suggests that a CaM-binding motif of TRPV1-CT forms an alpha helix that docks into the central cavity of CaM. (c) 2008 Elsevier Inc. All rights reserved.

引用

页码：680 / 683

页数：4

共 17 条

[1] Both the N-terminal loop and wing W2 of the forkhead domain of transcription factor FoxO4 are important for DNA binding [J].

Boura, Evzen ;

Silhan, Jan ;

Herman, Petr ;

Vecer, Jaroslav ;

Sulc, Miroslav ;

Teisinger, Jan ;

Obsilova, Veronika ;

Obsil, Tomas .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (11) :8265-8275

[2] The capsaicin receptor: a heat-activated ion channel in the pain pathway [J].

Caterina, MJ ;

Schumacher, MA ;

Tominaga, M ;

Rosen, TA ;

Levine, JD ;

Julius, D .

NATURE, 1997, 389 (6653) :816-824

[3] Coot:: model-building tools for molecular graphics [J].

Emsley, P ;

Cowtan, K .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 :2126-2132

[4] A closed compact structure of native Ca2+-calmodulin [J].

Fallon, JL ;

Quiocho, FA .

STRUCTURE, 2003, 11 (10) :1303-U7

[5] ATP binding site on the C-terminus of the vanilloid receptor [J].

Grycova, Lenka ;

Lansky, Zdenek ;

Friedlova, Eliska ;

Vlachova, Viktorie ;

Kubala, Martin ;

Obsilova, Veronika ;

Obsil, Tomas ;

Teisinger, Jan .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2007, 465 (02) :389-398

[6] SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling [J].

Guex, N ;

Peitsch, MC .

ELECTROPHORESIS, 1997, 18 (15) :2714-2723

[7] SOLUTION STRUCTURE OF CALMODULIN AND ITS COMPLEX WITH A MYOSIN LIGHT CHAIN KINASE FRAGMENT [J].

IKURA, M ;

BARBATO, G ;

KLEE, CB ;

BAX, A .

CELL CALCIUM, 1992, 13 (6-7) :391-400

[8]

Lakowicz J. R., 2006, PRINCIPLES FLUORESCE, DOI [10.1007/978-0-387-46312-4, DOI 10.1007/978-0-387-46312-4]

[9] Structural determinant of TRPV1 desensitization interacts with calmodulin [J].

Numazaki, M ;

Tominaga, T ;

Takeuchi, K ;

Murayama, N ;

Toyooka, H ;

Tominaga, M .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (13) :8002-8006

[10] Structure-function relationship of the TRP channel superfamily [J].

Owsianik, G. ;

D'hoedt, D. ;

Voets, T. ;

Nilius, B. .

REVIEWS OF PHYSIOLOGY BIOCHEMISTRY AND PHARMACOLOGY, VOL 156, 2006, 156 :61-90

← 1 2 →