1a7c
From Proteopedia
|
HUMAN PLASMINOGEN ACTIVATOR INHIBITOR TYPE-1 IN COMPLEX WITH A PENTAPEPTIDE
Overview
BACKGROUND: 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, ... [(full description)]
About this Structure
1A7C is a [Single protein] structure of sequence from [Homo sapiens] with NAG as [ligand]. Structure known Active Site: NUL. Full crystallographic information is available from [OCA].
Reference
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., Xue Y, Bjorquist P, Inghardt T, Linschoten M, Musil D, Sjolin L, Deinum J, Structure. 1998 May 15;6(5):627-36. PMID:9634700
Page seeded by OCA on Tue Oct 30 14:46:00 2007
