1PSI: Intact recombined alpha1-antitrypsin mutant PHE 51 to LEU

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1PSI: Intact recombined alpha1-antitrypsin mutant PHE 51 to LEU

JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)

ID	4531099
Author(s)	Abrahams, J. P.; Elliott, P. R.; Lomas, D. A.; Carrell, R. W.
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.
edoc-URL	https://edoc.unibas.ch/76002/
Full Text on edoc	No
Digital Object Identifier DOI	10.2210/pdb1psi/pdb
ISI-Number	2012136001729276
Document type (ISI)	Data set

20/04/2024

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