NDLI: Identification of residues contributing to the ATP binding site of Kir6.2

Content Provider	PubMed Central
Author	Trapp, Stefan Haider, Shozeb Jones, Phillippa Sansom, Mark S. P. Ashcroft, Frances M.
Copyright Year	2003
Abstract	The ATP-sensitive potassium (KATP) channel links cell metabolism to membrane excitability. Intracellular ATP inhibits channel activity by binding to the Kir6.2 subunit of the channel, but the ATP binding site is unknown. Using cysteine-scanning mutagenesis and charged thiol-modifying reagents, we identified two amino acids in Kir6.2 that appear to interact directly with ATP: R50 in the N-terminus, and K185 in the C-terminus. The ATP sensitivity of the R50C and K185C mutant channels was increased by a positively charged thiol reagent (MTSEA), and was reduced by the negatively charged reagent MTSES. Comparison of the inhibitory effects of ATP, ADP and AMP after thiol modification suggests that K185 interacts primarily with the β-phosphate, and R50 with the γ-phosphate, of ATP. A molecular model of the C-terminus of Kir6.2 (based on the crystal structure of Kir3.1) was constructed and automated docking was used to identify residues interacting with ATP. These results support the idea that K185 interacts with the β-phosphate of ATP. Thus both N- and C-termini may contribute to the ATP binding site.
Related Links	http://dx.doi.org/10.1093/emboj/cdg282
Ending Page	2912
Page Count	10
Starting Page	2903
File Format	PDF
ISSN	14602075
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	12
Volume Number	22
Language	English
Publisher	Oxford University Press
Publisher Date	2003-06-16
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

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

Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit

Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis

Identification of amino acid residues contributing to the pore of a P2X receptor.

Probing the ATP-binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis

Kir6.2 mutations causing neonatal diabetes prevent endocytosis of ATP-sensitive potassium channels

PKA-mediated phosphorylation of the human K(ATP) channel: separate roles of Kir6.2 and SUR1 subunit phosphorylation.

An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors

ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding

Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin

Identification of residues contributing to the ATP binding site of Kir6.2

Similar Documents

Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit

Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis

Identification of amino acid residues contributing to the pore of a P2X receptor.

Probing the ATP-binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis

Kir6.2 mutations causing neonatal diabetes prevent endocytosis of ATP-sensitive potassium channels

PKA-mediated phosphorylation of the human K(ATP) channel: separate roles of Kir6.2 and SUR1 subunit phosphorylation.

An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors

ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding

Identification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin

Identification of residues contributing to the ATP binding site of Kir6.2