Migration of PIP2 on KCNQ2 surface revealed by molecular dynamics simulations

Qiansen Zhang; Huaiyu Yang

doi:10.1007/978-1-4939-7362-0_12

Migration of PIP₂ on KCNQ2 surface revealed by molecular dynamics simulations

Qiansen Zhang
, Huaiyu Yang^*

^*Corresponding author for this work

School of Life Sciences

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

Abstract

Lipids and membrane proteins are the main components of cell membranes. Lipid-protein interactions are dynamic because these interactions typically occur on shallow protein surface clefts. Molecular dynamics (MD) simulations provide a tool for studying the dynamics of these interactions. Here, we describe the interactions of phosphatidylinositol-4,5-bisphosphate (PIP₂) with both the open and closed states of a KCNQ2 channel. Through these methods, we show that a lipid can migrate between different binding sites in a protein and this migration modulates protein functions.

Original language	English
Title of host publication	Methods in Molecular Biology
Publisher	Humana Press Inc.
Pages	151-161
Number of pages	11
DOIs	https://doi.org/10.1007/978-1-4939-7362-0_12
State	Published - 2018

Publication series

Name	Methods in Molecular Biology
Volume	1684
ISSN (Print)	1064-3745

Keywords

Lipid
Lipid-binding site
Lipid-protein interaction
Migration
Molecular dynamics simulation
PIP
Potassium channel

Access to Document

10.1007/978-1-4939-7362-0_12

Cite this

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abstract = "Lipids and membrane proteins are the main components of cell membranes. Lipid-protein interactions are dynamic because these interactions typically occur on shallow protein surface clefts. Molecular dynamics (MD) simulations provide a tool for studying the dynamics of these interactions. Here, we describe the interactions of phosphatidylinositol-4,5-bisphosphate (PIP2) with both the open and closed states of a KCNQ2 channel. Through these methods, we show that a lipid can migrate between different binding sites in a protein and this migration modulates protein functions.",

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AB - Lipids and membrane proteins are the main components of cell membranes. Lipid-protein interactions are dynamic because these interactions typically occur on shallow protein surface clefts. Molecular dynamics (MD) simulations provide a tool for studying the dynamics of these interactions. Here, we describe the interactions of phosphatidylinositol-4,5-bisphosphate (PIP2) with both the open and closed states of a KCNQ2 channel. Through these methods, we show that a lipid can migrate between different binding sites in a protein and this migration modulates protein functions.

KW - Lipid

KW - Lipid-binding site

KW - Lipid-protein interaction

KW - Migration

KW - Molecular dynamics simulation

KW - PIP

KW - Potassium channel

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PB - Humana Press Inc.

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