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

@article{citeulike:5973364, abstract = {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.}, author = {Grycova, Lenka and Lansky, Zdenek and Friedlova, Eliska and Obsilova, Veronika and Janouskova, Hana and Obsil, Tomas and Teisinger, Jan}, citeulike-article-id = {5973364}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.bbrc.2008.08.094}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18755153}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18755153}, day = {31}, doi = {10.1016/j.bbrc.2008.08.094}, issn = {1090-2104}, journal = {Biochemical and biophysical research communications}, keywords = {calmodulin, tesis, trpv1}, month = {October}, number = {4}, pages = {680--683}, posted-at = {2009-10-20 09:37:45}, priority = {2}, title = {Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin.}, url = {http://dx.doi.org/10.1016/j.bbrc.2008.08.094}, volume = {375}, year = {2008} }

TY - JOUR ID - citeulike:5973364 L3 - citeulike-article-id:5973364 N2 - 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. IS - 4 JF - Biochemical and biophysical research communications SN - 1090-2104 EP - 683 TI - Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin. VL - 375 SP - 680 KW - calmodulin KW - tesis KW - trpv1 AU - Grycova, Lenka AU - Lansky, Zdenek AU - Friedlova, Eliska AU - Obsilova, Veronika AU - Janouskova, Hana AU - Obsil, Tomas AU - Teisinger, Jan PY - 2008/10/31/ UR - http://dx.doi.org/10.1016/j.bbrc.2008.08.094 ER -