1psi
From Proteopedia
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'''INTACT RECOMBINED ALPHA1-ANTITRYPSIN MUTANT PHE 51 TO LEU''' | '''INTACT RECOMBINED ALPHA1-ANTITRYPSIN MUTANT PHE 51 TO LEU''' | ||
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[[Category: Elliott, P R.]] | [[Category: Elliott, P R.]] | ||
[[Category: Lomas, D A.]] | [[Category: Lomas, D A.]] | ||
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Revision as of 02:26, 3 May 2008
INTACT RECOMBINED ALPHA1-ANTITRYPSIN MUTANT PHE 51 TO LEU
Overview
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.
About this Structure
1PSI is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1PSI with [Serpins]. Full crystallographic information is available from OCA.
Reference
Inhibitory conformation of the reactive loop of alpha 1-antitrypsin., Elliott PR, Lomas DA, Carrell RW, Abrahams JP, Nat Struct Biol. 1996 Aug;3(8):676-81. PMID:8756325 Page seeded by OCA on Sat May 3 05:26:16 2008
