Open AccessCrystallization and preliminary X‐ray structural studies of human prouroguanylin
Author(s) -
Ito Len,
Hidaka Yuji,
Okumura Masaki,
Konishi Hironori,
Yamaguchi Hiroshi
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108013444
Subject(s) - crystallization , crystallography , x ray crystallography , diffraction , chemistry , folding (dsp implementation) , resolution (logic) , ligand (biochemistry) , diffusion , biochemistry , receptor , physics , optics , organic chemistry , thermodynamics , electrical engineering , artificial intelligence , computer science , engineering
Uroguanylin, which serves as an endogenous ligand of guanylyl cyclase C, is initially secreted in the form of a precursor, prouroguanylin. The N‐terminal region of prouroguanylin interacts with the mature portion of prouroguanylin during the folding pathway. Here, a preliminary X‐ray crystallographic study of prouroguanylin is presented. Prouroguanylin was refolded, purified and crystallized using the hanging‐drop vapour‐diffusion method. Prouroguanylin crystals were cryocooled and used for data collection. The diffraction data showed that the crystals belonged to space group P 6 1 22, with unit‐cell parameters a = b = 55.6, c = 157.7 Å, and diffracted to 2.5 Å resolution. The structure is currently being analyzed.