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Reactivity of basic amino acid pairs in prohormone processing: model of pro-ocytocin/neurophysin processing domain.
- Source :
-
Archives of biochemistry and biophysics [Arch Biochem Biophys] 2007 Jul 15; Vol. 463 (2), pp. 231-6. Date of Electronic Publication: 2007 Apr 05. - Publication Year :
- 2007
-
Abstract
- Statistical analysis of several potential dibasic cleavage sites reveals differences in the distribution of basic doublets when the in vivo cleaved sites were compared to those which are not cleaved. Analysis of the substrate specificity of protease Kex2 towards the pro-ocytocin/neurophysin processing domain (pro-OT/Np(7-15) with altered basic pairs shows a cleavage efficiency order in accord with the statistical data. Structural analysis of these substrates indicates that each basic pair is associated with a local and specific conformational change. Thus, the in vivo cleavage hierarchy of dibasic sites is encoded by both the nature of basic pairs and the plasticity of proteolytic processing domains.
- Subjects :
- Amino Acids, Basic analysis
Circular Dichroism
Kinetics
Neurophysins metabolism
Oxytocin metabolism
Proprotein Convertases metabolism
Protein Precursors metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Substrate Specificity
Amino Acids, Basic chemistry
Neurophysins chemistry
Oxytocin chemistry
Protein Precursors chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0003-9861
- Volume :
- 463
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Archives of biochemistry and biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 17467653
- Full Text :
- https://doi.org/10.1016/j.abb.2007.03.014