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CRYO-EM TRPV5 SIGNED

Structure-function analysis of the calcium channel TRPV5

Total Cost €

EC-Contrib. €

Partnership

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Outcomes and
results

CRYO-EM TRPV5 project word cloud

Explore the words cloud of the CRYO-EM TRPV5 project. It provides you a very rough idea of what is the project "CRYO-EM TRPV5" about.

inactivation particle category vanilloid view trp intramolecular structure elucidation activation connecting elucidate unravel single biology insights voltage messengers familiy molecular domains cheng plasma integral ionic biophysical regulation channel background limited ultimately incompletely flow selective liposomes structural ligands protein pore membrane forms ions distinctive packages channels reconstitution extrapolated receptor em expertise proteins mechanistic permeability functioning selectivity nanodiscs dependent first functional differences critical ion permeation 3d trpv5 cryo function intracellular prof mechanism lipid transient calcium gating hydrophillic

Project "CRYO-EM TRPV5" data sheet

The following table provides information about the project.

Coordinator	STICHTING KATHOLIEKE UNIVERSITEIT Organization address address: GEERT GROOTEPLEIN NOORD 9 city: NIJMEGEN postcode: 6525 EZ website: www.radboudumc.nl contact info title: n.a. name: n.a. surname: n.a. function: n.a. email: n.a. telephone: n.a. fax: n.a.
Coordinator Country	Netherlands [NL]
Project website	https://www.radboudumc.nl/en/people/jenny-van-der-wijst
Total cost	162˙864 €
EC max contribution	162˙864 € (100%)
Programme	1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
Code Call	H2020-MSCA-IF-2016
Funding Scheme	MSCA-IF-GF
Starting year	2017
Duration (year-month-day)	from 2017-09-01 to 2020-04-12

Partnership

Take a look of project's partnership.

#	participants	country	role	EC contrib. [€]
1	STICHTING KATHOLIEKE UNIVERSITEIT STICHTING KATHOLIEKE UNIVERSITEIT Organization address address: GEERT GROOTEPLEIN NOORD 9 city: NIJMEGEN postcode: 6525 EZ website: www.radboudumc.nl contact info title: n.a. name: n.a. surname: n.a. function: n.a. email: n.a. telephone: n.a. fax: n.a.	NL (NIJMEGEN)	coordinator	162˙864.00
2	THE REGENTS OF THE UNIVERSITY OF CALIFORNIA THE REGENTS OF THE UNIVERSITY OF CALIFORNIA Organization address address: FRANKLIN STREET 1111, 12 FLOOR city: OAKLAND CA postcode: 94607 website: http://www.universityofcalifornia.edu/ contact info title: n.a. name: n.a. surname: n.a. function: n.a. email: n.a. telephone: n.a. fax: n.a.	US (OAKLAND CA)	partner	0.00

Map

Project objective

Ion channels are proteins composed of a hydrophillic pore that facilitate ion flow across a plasma membrane. This ionic permeability is controlled by a set of essential properties affecting the channel activation and inactivation in response to voltage, ligands, or intracellular second messengers. The focus of the present project proposal, the transient receptor potential vanilloid channel (TRPV5), forms a specific category within the large TRP familiy of ion channels as it comprises a unique high selectivity for calcium ions together with a calcium-dependent inactivation mechanism that is incompletely understood. Detailed analysis of the TRPV5 channel will provide new structural insights into channel gating that can be extrapolated to other TRP channels, as the current knowledge on the TRP protein structure and its impact on the regulation of the channel function is still limited. The key objective of my project is to deliver the first detailed mechanistic view of TRPV5 by connecting Prof. Cheng’s expertise in structural biology with my biophysical background on TRP channel functioning. The following work packages will be addressed: 1) Channel activation mechanism of TRPV5 Elucidation of the 3D structure of integral TRPV5 by single-particle cryo-EM will provide critical structural and mechanistic insight into calcium-dependent regulation of channel function. 2) Intramolecular regulation of TRPV5 Reconstitution of TRPV5 into lipid nanodiscs and liposomes allows detailed study on lipid regulation and the mechanism of channel inactivation Taken together, this project focuses on the structure-function analysis of TRPV5, a distinctive calcium-selective TRP channel. The goal is to elucidate the structure of the TRPV5 channel, and to unravel functional domains that are involved in channel function at the mechanistic level. This will ultimately advance our understanding of the molecular differences of activation, ion permeation and gating of TRP channels.

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