Sökning: onr:"swepub:oai:DiVA.org:umu-3836" >
The spontaneous pol...
The spontaneous polymerization of plasminogen activator inhibitor type-2 and Z-antitrypsin are due to different molecular aberrations
-
- Wilczynska, Malgorzata (författare)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
-
- Lobov, Sergei (författare)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
-
- Ny, Tor (författare)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
-
(creator_code:org_t)
- 2003
- 2003
- Engelska.
-
Ingår i: FEBS Letters. - 0014-5793 .- 1873-3468. ; 537:1-3, s. 11-16
- Relaterad länk:
-
https://urn.kb.se/re...
-
visa fler...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- The wild-type form of plasminogen activator inhibitor type-2 (PAI-2) and the pathogenic Z-mutant of alpha(1)-antitrypsin (alpha(1)AT) are serpins that spontaneously polymerize by the loop-sheet mechanism. Compared to the consensus serpin sequence, both PAI-2 and Z-alpha(1)AT have deviations in the so-called breach region located at the top of the A beta-sheet. In the case of Z-alpha(1)AT, conformational perturbations caused by a single amino acid substitution result in polymerization in vivo and predisposes to disease. To test whether the polymerization of PAI-2 is due to aberrations in the breach region, we constructed substitution mutants of PAI-2 with conserved residues in this region. Analysis of the mutants revealed that deviations in the breach region modulate but are not the major cause of PAI-2 polymerization. Rather, PAI-2 exists in a highly polymerogenic conformation and does not require conformational rearrangements before polymerization can take place.
Nyckelord
- Serpin
- Loop–sheet polymerization
- Plasminogen activator inhibitor type-2
- MEDICINE
- MEDICIN
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas