Crystallization and preliminary X-ray structural studies of human prouroguanylin

Len Ito, Yuji Hidaka, Masaki Okumura, Hironori Konishi, Hiroshi Yamaguchi

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


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 P6122, 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.

Original languageEnglish
Pages (from-to)531-532
Number of pages2
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number6
Publication statusPublished - 2008
Externally publishedYes


  • Peptide hormones
  • Precursor proteins
  • Prouroguanylin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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