1PSI: Intact recombined alpha1-antitrypsin mutant PHE 51 to LEU
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4531099
Author(s) Abrahams, JP; Elliott, PR; Lomas, DA; Carrell, RW
Author(s) at UniBasel Abrahams, Jan Pieter
Year 1996
Title 1PSI: Intact recombined alpha1-antitrypsin mutant PHE 51 to LEU
Journal Worldwide Protein Data Bank
Pages / Article-Number 1PSI
Keywords serine protease inhibitor
Mesh terms Science & TechnologyLife Sciences & BiomedicineBiochemistry & Molecular BiologyBiochemistry & Molecular Biology
Abstract

The reactive site loop of the serpin family of serine proteinase inhibitors is flexible and can adopt a number of diverse conformations. A 2.9 A resolution structure of alpha 1-antitrypsin-the principal proteinase inhibitor in human plasma-shows the loop in a stable canonical conformation matching that found in all other families of serine proteinase inhibitors. This unexpected finding in the absence of loop insertion into the body of the molecule favours a two-stage mechanism of inhibition and provides a model for the heparin activation of antithrombin. The beta-pleated strand conformation of the loop also accounts for the polymerization of the serpins in disease and for their association with other beta-sheet structures, most notably the beta-amyloid of Alzheimer's disease.

Full Text on edoc
Digital Object Identifier DOI 10.2210/pdb1psi/pdb
ISI-Number DRCI:DATA2012136001729276
Document type (ISI) Data set
   

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