Crystallization and preliminary X-ray crystallographic analysis of rat calcineurin B homologous protein 1

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Youichi NaoeToshiyuki Shimizu

Abstract

Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding protein that plays a role in membrane trafficking and binds to multiple effector proteins, including Na+/H+ exchangers, serine/threonine protein kinase and calcineurin, potentially modulating their function. CHP1 has been crystallized at 277 K using polyethylene glycol as a precipitant. The crystal belongs to space group P2(1), with unit-cell parameters a = 55.5, b = 38.5, c = 90.0 A, beta = 90.7 degrees. A full set of diffraction data was collected to 2.2 A resolution at 100 K using the Photon Factory synchrotron-radiation source.

References

Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Apr 26, 1996·The Journal of Biological Chemistry·M R BarrosoE S Sztul
Oct 29, 1996·Proceedings of the National Academy of Sciences of the United States of America·X Lin, D L Barber
Dec 14, 1999·The Journal of Biological Chemistry·X LinD L Barber
May 15, 2001·The Journal of Biological Chemistry·T PangM Shigekawa
Sep 3, 2002·Journal of Biochemistry·Norihiro NakamuraHiroshi Kanazawa

❮ Previous
Next ❯

Citations

Jul 1, 2005·The Journal of Biological Chemistry·Youichi NaoeToshiyuki Shimizu

❮ Previous
Next ❯

Related Concepts

Related Feeds

ApoE, Lipids & Cholesterol

Serum cholesterol, triglycerides, apolipoprotein B (APOB)-containing lipoproteins (very low-density lipoprotein (VLDL), immediate-density lipoprotein (IDL), and low-density lipoprotein (LDL), lipoprotein A (LPA)) and the total cholesterol/high-density lipoprotein (HDL) cholesterol ratio are all connected in diseases. Here is the latest research.