1A7C

HUMAN PLASMINOGEN ACTIVATOR INHIBITOR TYPE-1 IN COMPLEX WITH A PENTAPEPTIDE

Summary for 1A7C

• Entry DOI: 10.2210/pdb1a7c/pdb
• Descriptor: PLASMINOGEN ACTIVATOR INHIBITOR TYPE 1, PENTAPEPTIDE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-D-ribopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: serine protease inhibitor, pai-1, carbohydrate, inhibitor complex, protease inhibitor-peptide complex, hydrolase inhibitor-peptide complex, hydrolase inhibitor/peptide
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 44629.88

Authors

Xue, Y.,Inghardt, T.,Sjolin, L.,Deinum, J. (deposition date: 1998-03-12, release date: 1999-03-23, Last modification date: 2024-10-30)

Primary citation

Xue, Y.,Bjorquist, P.,Inghardt, T.,Linschoten, M.,Musil, D.,Sjolin, L.,Deinum, J.
Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide
Structure, 6:627-636, 1998

PubMed Abstract: Plasminogen activator inhibitor type 1 (PAI-1) is an important endogenous regulator of the fibrinolytic system. Reduction of PAI-1 activity has been shown to enhance dissolution of blood clots. Like other serpins, PAI-1 binds covalently to a target serine protease, thereby irreversibly inactivating the enzyme. During this process the exposed reactive-centre loop of PAI-1 is believed to undergo a conformational change becoming inserted into beta sheet A of the serpin. Incubation with peptides from the reactive-centre loop transform serpins into a substrate for their target protease. It has been hypothesised that these peptides bind to beta sheet A, thereby hindering the conformational rearrangement leading to loop insertion and formation of the stable serpin-protease complex.

PubMed: 9634700
DOI: 10.1016/S0969-2126(98)00064-1

Experimental method

X-RAY DIFFRACTION (1.95 Å)