Sequence-Specific 1H NMR Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B

Josep Vendrell, Gerhard Wider, Kurt Wüthrich, Francesc X. Avilés

Sortida de recercaRecercarevisió per companys

9 Cites (Scopus)

Resum

Nearly complete sequence-specific 1Η NMR assignments are presented for amino acid residues 3-81 in the 81-residue globular activation domain of porcine pancreatic procarboxypeptidase B isolated after limited tryptic proteolysis of the zymogen. These resonance assignments are consistent with the chemically determined amino acid sequence. Regular secondary structure elements were identified from nuclear Overhauser effects and the sequence locations of slowly exchanging backbone amide protons. The molecule contains two α-helices, including residues 20-30 and approximately residues 58-72, and a three-stranded antiparallel β-sheet with the individual strands extending approximately from 12 to 17, 50 to 55, and 75 to 77. The identification of these secondary structures and a preliminary analysis of additional long-range NOE distance constraints show that isolated activation domain B forms a stable structure with the typical traits of a globular protein. The data presented here are the basis for the determination of the complete three-dimensional structure of activation domain B, which is currently in progress. © 1990, American Chemical Society. All rights reserved.
Idioma originalEnglish
Pàgines (de-a)7515-7522
RevistaBiochemistry
Volum29
DOIs
Estat de la publicacióPublicada - 1 d’ag. 1990

Empremta digital Navegar pels temes de recerca de 'Sequence-Specific <sup>1</sup>H NMR Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B'. Junts formen una empremta única.

Citeu això