These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Involvement of the NH2-terminal region of oryzacystatin-I in cysteine proteinase inhibition.
    Author: Urwin PE, Atkinson HJ, McPherson MJ.
    Journal: Protein Eng; 1995 Dec; 8(12):1303-7. PubMed ID: 8869643.
    Abstract:
    Cystatins are small protein inhibitors of cysteine proteinases. The relative importance of the N-terminal region of cystatins, and of a conserved glycine within this region, remains unclear despite several studies. It was found that deletion of the N-terminal 21 amino acids abolishes the inhibitory capacity of oryzacystatin-I. The importance of a conserved glycine residue (Gly10) was also examined by replacing it with 11 other amino acids. Three further glycine residues (Gly5, -6 and -11) in this N-terminal region of oryzacystatin-I were similarly mutated. Only those variants in which Gly10 was substituted show any significant change in inhibitory capacity compared with wild-type oryzacystatin-I. The inhibitory characteristics of hybrid cystatin molecules comprising regions of chicken egg white cystatin and oryzacystatin were also examined. It is suggested that in common with animal cystatins, the N-terminal region of the plant cystatin, oryzacystatin-I, and in particular the highly conserved Gly10 residue are important for effective inhibition of papain.
    [Abstract] [Full Text] [Related] [New Search]