1D5S

CRYSTAL STRUCTURE OF CLEAVED ANTITRYPSIN POLYMER

Summary for 1D5S

• Entry DOI: 10.2210/pdb1d5s/pdb
• Descriptor: P1-ARG ANTITRYPSIN (2 entities in total)
• Functional Keywords: serpin fold, rcl cleavage, a beta sheet polymerisation, hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted. Short peptide from AAT: Secreted, extracellular space, extracellular matrix: P01009 P01009
• Total number of polymer chains: 2
• Total formula weight: 42342.39

Authors

Dunstone, M.A.,Dai, W.,Whisstock, J.C.,Rossjohn, J.,Pike, R.N.,Feil, S.C.,Le Bonneic, B.F.,Parker, M.W.,Bottomley, S.P. (deposition date: 1999-10-11, release date: 2000-04-02, Last modification date: 2024-02-07)

Primary citation

Dunstone, M.A.,Dai, W.,Whisstock, J.C.,Rossjohn, J.,Pike, R.N.,Feil, S.C.,Le Bonniec, B.F.,Parker, M.W.,Bottomley, S.P.
Cleaved antitrypsin polymers at atomic resolution.
Protein Sci., 9:417-420, 2000

PubMed Abstract: Alpha1-antitrypsin deficiency, which can lead to both emphysema and liver disease, is a result of the accumulation of alpha1-antitrypsin polymers within the hepatocyte. A wealth of biochemical and biophysical data suggests that alpha1-antitrypsin polymers form via insertion of residues from the reactive center loop of one molecule into the beta-sheet of another. However, this long-standing hypothesis has not been confirmed by direct structural evidence. Here, we describe the first crystallographic evidence of a beta-strand linked polymer form of alpha1-antitrypsin: the crystal structure of a cleaved alpha1-antitrypsin polymer.

PubMed: 10716194

Experimental method

X-RAY DIFFRACTION (3 Å)