Reactivity of basic amino acid pairs in prohormone processing: model of pro-ocytocin/neurophysin processing domain
Details
Serval ID
serval:BIB_D00E93D3405B
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Reactivity of basic amino acid pairs in prohormone processing: model of pro-ocytocin/neurophysin processing domain
Journal
Archives of Biochemistry and Biophysics
ISSN
0003-9861 (Print)
Publication state
Published
Issued date
07/2007
Volume
463
Number
2
Pages
231-6
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jul 15
Research Support, Non-U.S. Gov't --- Old month value: Jul 15
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.
Keywords
Amino Acids, Basic/analysis/*chemistry
Circular Dichroism
Kinetics
Neurophysins/*chemistry/metabolism
Oxytocin/*chemistry/metabolism
Proprotein Convertases/metabolism
Protein Precursors/*chemistry/metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Substrate Specificity
Pubmed
Web of science
Create date
28/01/2008 11:35
Last modification date
20/08/2019 16:50