Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na+/H+ exchanger NHE1

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Youssef Ben AmmarShigeo Wakabayashi

Abstract

Calcineurin homologous protein (CHP) is a Ca2+-binding protein that directly interacts with and regulates the activity of all plasma-membrane Na+/H+-exchanger (NHE) family members. In contrast to the ubiquitous isoform CHP1, CHP2 is highly expressed in cancer cells. To understand the regulatory mechanism of NHE1 by CHP2, the complex CHP2-NHE1 (amino acids 503-545) has been crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as precipitant. The crystals diffract to 2.7 A and belong to a tetragonal space group, with unit-cell parameters a = b = 49.96, c = 103.20 A.

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Citations

May 19, 2009·The Journal of Experimental Biology·Mark DonowitzXuhang Li
Mar 20, 2013·Molecular Aspects of Medicine·Mark DonowitzDaniel Fuster
May 20, 2006·The EMBO Journal·Youssef Ben AmmarShigeo Wakabayashi
Jul 7, 2007·Physiological Reviews·Mark Donowitz, Xuhang Li
Jul 21, 2020·Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine·Wayne Taylor CottleJoseph John Provost
Nov 21, 2019·Current Molecular Medicine·Wenhui WangJinming Li
Jan 9, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Shuo LiangCarola Hunte
Oct 9, 2020·Applied Immunohistochemistry & Molecular Morphology : AIMM·Liqin XuJian Feng

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