1psi
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INTACT RECOMBINED ALPHA1-ANTITRYPSIN MUTANT PHE 51 TO LEU
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Emphysema OMIM:[107400], Emphysema-cirrhosis OMIM:[107400], Hemorrhagic diathesis due to antithrombin Pittsburgh OMIM:[107400], Pulmonary disease, chronic obstructive, susceptibility to OMIM:[107400]
About this StructureAbout this Structure
1PSI is a Single protein structure of sequence from Homo sapiens with SCC as ligand. The following page contains interesting information on the relation of 1PSI with [Serpins]. Full crystallographic information is available from OCA.
ReferenceReference
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
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