Crystallization and preliminary X-ray structural studies of human prouroguanylin.
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 P6(1)22, with unit-cell parameters a = b = 55.6, c = 157.7 A, and diffracted to 2.5 A resolution. The structure is currently being analyzed.
Ito
Len
L
School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan.
Hidaka
Yuji
Y
Okumura
Masaki
M
Konishi
Hironori
H
Adermann
Knut
K
Yamaguchi
Hiroshi
H
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D018076:DNA, Complementary; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D002479:Inclusion Bodies / Q000737:chemistry; D008969:Molecular Sequence Data; D009154:Mutation; D017510:Protein Folding; D011498:Protein Precursors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012995:Solubility; D014961:X-Ray Diffraction
D018076:DNA, Complementary; D011498:Protein Precursors; D011994:Recombinant Proteins; C097400:prouroguanylin