6 research outputs found
Structural insights on TRPV5 gating by endogenous modulators.
- Author
- Publication venue
- eScholarship, University of California
- Publication date
- 01/10/2018
- Field of study
TRPV5 is a transient receptor potential channel involved in calcium reabsorption. Here we investigate the interaction of two endogenous modulators with TRPV5. Both phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and calmodulin (CaM) have been shown to directly bind to TRPV5 and activate or inactivate the channel, respectively. Using cryo-electron microscopy (cryo-EM), we determined TRPV5 structures in the presence of dioctanoyl PI(4,5)P2 and CaM. The PI(4,5)P2 structure reveals a binding site between the N-linker, S4-S5 linker and S6 helix of TRPV5. These interactions with PI(4,5)P2 induce conformational rearrangements in the lower gate, opening the channel. The CaM structure reveals two TRPV5 C-terminal peptides anchoring a single CaM molecule and that calcium inhibition is mediated through a cation-Ď€ interaction between Lys116 on the C-lobe of calcium-activated CaM and Trp583 at the intracellular gate of TRPV5. Overall, this investigation provides insight into the endogenous modulation of TRPV5, which has the potential to guide drug discovery
Recommended from our members
Structural insights on TRPV5 gating by endogenous modulators.
- Author
- Publication venue
- eScholarship, University of California
- Publication date
- 01/10/2018
- Field of study
TRPV5 is a transient receptor potential channel involved in calcium reabsorption. Here we investigate the interaction of two endogenous modulators with TRPV5. Both phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and calmodulin (CaM) have been shown to directly bind to TRPV5 and activate or inactivate the channel, respectively. Using cryo-electron microscopy (cryo-EM), we determined TRPV5 structures in the presence of dioctanoyl PI(4,5)P2 and CaM. The PI(4,5)P2 structure reveals a binding site between the N-linker, S4-S5 linker and S6 helix of TRPV5. These interactions with PI(4,5)P2 induce conformational rearrangements in the lower gate, opening the channel. The CaM structure reveals two TRPV5 C-terminal peptides anchoring a single CaM molecule and that calcium inhibition is mediated through a cation-Ď€ interaction between Lys116 on the C-lobe of calcium-activated CaM and Trp583 at the intracellular gate of TRPV5. Overall, this investigation provides insight into the endogenous modulation of TRPV5, which has the potential to guide drug discovery
Characterization of a factor H mutation that perturbs the alternative pathway of complement in a family with membranoproliferative GN
- Author
- Publication venue
- 'American Society of Nephrology (ASN)'
- Publication date
- 10/04/2014
- Field of study
Complement C3 activation is a characteristic finding in membranoproliferative GN (MPGN). This activation can be caused by immune complex deposition or an acquired or inherited defect in complement regulation. Deficiency of complement factor H has long been associated with MPGN. More recently, heterozygous genetic variants have been reported in sporadic cases of MPGN, although their functional significance has not been assessed. We describe a family with MPGN and acquired partial lipodystrophy. Although C3 nephritic factor was shown in family members with acquired partial lipodystrophy, it did not segregate with the renal phenotype. Genetic analysis revealed a novel heterozygous mutation in complement factor H (R83S) in addition to known risk polymorphisms carried by individuals with MPGN. Patients with MPGN had normal levels of factor H, and structural analysis of the mutant revealed only subtle alterations. However, functional analysis revealed profoundly reduced C3b binding, cofactor activity, and decay accelerating activity leading to loss of regulation of the alternative pathway. In summary, this family showed a confluence of common and rare functionally significant genetic risk factors causing disease. Data from our analysis of these factors highlight the role of the alternative pathway of complement in MPGN
Characterization of a Factor H Mutation That Perturbs the Alternative Pathway of Complement in a Family with Membranoproliferative GN
- Author
- Alison Macleod
- Andrew P. Herbert
- Ann Humphrey
- Anna Richards
- Bolton
- Claire L. Harris
- Daha
- Daniel Ahlert
- David Kavanagh
- Edwin K.S. Wong
- Finn
- Geisilaine S. Reis
- Holly E. Anderson
- James O. Tellez
- Kevin J. Marchbank
- Lisa Strain
- Mauro Santibanez-Koref
- Nicholas Fluck
- Paul Brown
- Paul N. Barlow
- Power
- Rachel C. Challis
- Scott
- Thompson
- Timothy H.J. Goodship
- Publication venue
- 'American Society of Nephrology (ASN)'
- Publication date
- Field of study
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- Y.E. Young
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Chen
- Y.F. Qi
- Y.H. Cha
- Y.H. Tsang
- Y.J. Cai
- Y.J. Chen
- Y.J. Cheng
- Y.J. Deng
- Y.J. Dong
- Y.J. Zhang
- Y.K. Kuo
- Y.K. Kuo
- Y.K. Kuo
- Y.K. Park
- Y.L. Li
- Y.L. Li
- Y.L. Li
- Y.L. Sun
- Y.M. Chang
- Y.M. Chen
- Y.M. Liu
- Y.M. Liu
- Y.N. Xu
- Y.P. Huo
- Y.P. Tong
- Y.S. Liu
- Y.V. Volk
- Y.W. Lee
- Y.X. Fan
- Y.X. Zhao
- Y.Y. Lin
- Yu. Nizienko
- Z. Burshtein
- Z. Dai
- Z. Hricha
- Z. Li
- Z. Zeng
- Z. Zhang
- Z.A. Yasa
- Z.G. Zhang
- Z.G. Zhang
- Z.G. Zhang
- Z.H.H. Yang
- Z.L. Liu
- Z.P. Sun
- Z.P. Sun
- Z.T. Chen
- Z.Y. Li
- Z.z. Xu
- Zs. Bor
- Zs. Bor
- {Sect. 6.13.5}
- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- 01/01/2007
- Field of study