1PSI

Intact recombined alpha1-antitrypsin mutant PHE 51 to LEU

Summary for 1PSI

• Entry DOI: 10.2210/pdb1psi/pdb
• Descriptor: ALPHA=1=-ANTITRYPSIN (1 entity in total)
• Functional Keywords: serpin, serine protease inhibitor, glycoprotein, polymorphism, emphysema, disease mutation, acute phase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted. Short peptide from AAT: Secreted, extracellular space, extracellular matrix: P01009
• Total number of polymer chains: 1
• Total formula weight: 44406.54

Authors

Abrahams, J.P.,Elliott, P.R.,Lomas, D.A.,Carrell, R.W. (deposition date: 1996-06-11, release date: 1996-12-07, Last modification date: 2023-08-09)

Primary citation

Elliott, P.R.,Lomas, D.A.,Carrell, R.W.,Abrahams, J.P.
Inhibitory conformation of the reactive loop of alpha 1-antitrypsin.
Nat.Struct.Biol., 3:676-681, 1996

PubMed 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.

PubMed: 8756325
DOI: 10.1038/nsb0896-676

Experimental method

X-RAY DIFFRACTION (2.92 Å)