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Crystallization and preliminary X-ray structural studies of human prouroguanylin.

ABSTRACT: 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.

SUBMITTER: Ito L

PROVIDER: S-EPMC2496868 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray structural studies of human prouroguanylin.

Ito Len L Hidaka Yuji Y Okumura Masaki M Konishi Hironori H Adermann Knut K Yamaguchi Hiroshi H

Acta crystallographica. Section F, Structural biology and crystallization communications 20080523 Pt 6

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 ...[more]

PMID: 18540068

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