Literature DB >> 3426597

Conformational predictive studies on the activation segment of pancreatic procarboxypeptidases.

M Vilanova1, F X Avilés, J Vendrell, E Méndez.   

Abstract

Little is known about the conformation and evolutionary origin of the activation segment of pancreatic procarboxypeptidases. Analysis of the sequence and secondary structure propensities of these propeptide segments indicate that they contain two regions structurally related to the Ca2+-binding sites of the EF-hand protein family. This proposed homology could explain how (and why) carboxypeptidases developed such long (94 residues) activation peptides.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3426597     DOI: 10.1016/0006-291x(87)90428-1

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  1H-n.m.r. studies of the isolated activation segment from pig procarboxypeptidase A.

Authors:  J Vendrell; F X Avilés; M Vilanova; C H Turner; C Crane-Robinson
Journal:  Biochem J       Date:  1990-04-01       Impact factor: 3.857

2.  Analysis of the conformation and ligand-binding properties of the activation segment of pig procarboxypeptidase A.

Authors:  M Vilanova; J Vendrell; C M Cuchillo; F X Avilés
Journal:  Biochem J       Date:  1988-05-01       Impact factor: 3.857

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.