NDLI: Identification of the Conformational transition pathway in PIP2 Opening Kir Channels

Content Provider	PubMed Central
Author	Li, Junwei Lü, Shouqin Liu, Yuzhi Pang, Chunli Chen, Yafei Zhang, Suhua Yu, Hui Long, Mian Zhang, Hailin Logothetis, Diomedes E. Zhan, Yong An, Hailong
Copyright Year	2015
Abstract	The gating of Kir channels depends critically on phosphatidylinositol 4,5-bisphosphate (PIP2), but the detailed mechanism by which PIP2 regulates Kir channels remains obscure. Here, we performed a series of Targeted molecular dynamics simulations on the full-length Kir2.1 channel and, for the first time, were able to achieve the transition from the closed to the open state. Our data show that with the upward motion of the cytoplasmic domain (CTD) the structure of the C-Linker changes from a loop to a helix. The twisting of the C-linker triggers the rotation of the CTD, which induces a small downward movement of the CTD and an upward motion of the slide helix toward the membrane that pulls the inner helix gate open. At the same time, the rotation of the CTD breaks the interaction between the CD- and G-loops thus releasing the G-loop. The G-loop then bounces away from the CD-loop, which leads to the opening of the G-loop gate and the full opening of the pore. We identified a series of interaction networks, between the N-terminus, CD loop, C linker and G loop one by one, which exquisitely regulates the global conformational changes during the opening of Kir channels by PIP2.
Related Links	http://dx.doi.org/10.1038/srep11289
Starting Page	11289
File Format	PDF
ISSN	20452322
e-ISSN	20452322
Journal	Scientific Reports
Volume Number	5
Language	English
Publisher	Nature Publishing Group
Publisher Date	2015-06-01
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Science and technology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker

PIP2-Binding Site in Kir Channels: Definition by Multiscale Biomolecular Simulations†

The ICl,swell inhibitor DCPIB blocks Kir channels that possess weak affinity for PIP2

Conformational Transition Pathway in the Activation Process of Allosteric Glucokinase

A sodium-mediated structural switch that controls the sensitivity of Kir channels to PIP2

Conformational transition pathway in the allosteric process of human glucokinase

Human EAG channels are directly modulated by PIP2 as revealed by electrophysiological and optical interference investigations

Dissection of the components for PIP2 activation and thermosensation in TRP channels

Inter-Subunit Interactions across the Upper Voltage Sensing-Pore Domain Interface Contribute to the Concerted Pore Opening Transition of Kv Channels

Identification of the Conformational transition pathway in PIP2 Opening Kir Channels

Similar Documents

PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4–S5 linker

PIP2-Binding Site in Kir Channels: Definition by Multiscale Biomolecular Simulations†

The ICl,swell inhibitor DCPIB blocks Kir channels that possess weak affinity for PIP2

Conformational Transition Pathway in the Activation Process of Allosteric Glucokinase

A sodium-mediated structural switch that controls the sensitivity of Kir channels to PIP2

Conformational transition pathway in the allosteric process of human glucokinase

Human EAG channels are directly modulated by PIP2 as revealed by electrophysiological and optical interference investigations

Dissection of the components for PIP2 activation and thermosensation in TRP channels

Inter-Subunit Interactions across the Upper Voltage Sensing-Pore Domain Interface Contribute to the Concerted Pore Opening Transition of Kv Channels

Identification of the Conformational transition pathway in PIP2 Opening Kir Channels