Open AccessCrystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na + /H + exchanger NHE1
Author(s) -
Ben Ammar Youssef,
Takeda Soichi,
Miyano Masashi,
Sugawara Mitsuaki,
Mori Hidezo,
Wakabayashi Shigeo
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105030836
Subject(s) - crystallization , crystallography , chemistry , homologous chromosome , cytoplasm , biochemistry , gene , organic chemistry
Calcineurin homologous protein (CHP) is a Ca 2+ ‐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 Å and belong to a tetragonal space group, with unit‐cell parameters a = b = 49.96, c = 103.20 Å.