ArticleProtein science : a publication of the Protein Society2011
Metals affect the structure and activity of human plasminogen activator inhibitor-1. II. Binding affinity and conformational changes.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Dissecting molecular details and functional effects of the high-affinity copper binding site in plasminogen activator Inhibitor-1.Protein science : a publication of the Protein Society · 2021Article
- Targeting PAI-1 in Cardiovascular Disease: Structural Insights Into PAI-1 Functionality and Inhibition.Frontiers in cardiovascular medicine · 2020Review
- Resolving distinct molecular origins for copper effects on PAI-1.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Single fluorescence probes along the reactive center loop reveal site-specific changes during the latency transition of PAI-1.Protein science : a publication of the Protein Society · 2016Article
- Application of long-acting VLHL PAI-1 during sutureless partial nephrectomy in mice reduces bleeding.BioMed research international · 2015Article
- Zn2+ mediates high affinity binding of heparin to the αC domain of fibrinogen.The Journal of biological chemistry · 2013Article
- Crystal structure of plasminogen activator inhibitor-1 in an active conformation with normal thermodynamic stability.The Journal of biological chemistry · 2011Article
- Metals affect the structure and activity of human plasminogen activator inhibitor-1. I. Modulation of stability and protease inhibition.Protein science : a publication of the Protein Society · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human plasminogen activator inhibitor type 1 (PAI-1) is a serine protease inhibitor with a metastable active conformation. The lifespan of the active form of PAI-1 is modulated via interaction with the plasma protein, vitronectin, and various metal ions. These metal ions fall into two categories: Type I metals, including calcium, magnesium, and manganese, stabilize PAI-1 in the absence of vitronectin, whereas Type II metals, including cobalt, copper, and nickel, destabilize PAI-1 in the absence of vitronectin, but stabilize PAI-1 in its presence. To provide a mechanistic basis for understanding the unusual modulation of PAI-1 structure and activity, the binding characteristics and conformational effects of these two types of metals were further evaluated. Steady-state binding measurements using surface plasmon resonance indicated that both active and latent PAI-1 exhibit a dissociation constant in the low micromolar range for binding to immobilized nickel. Stopped-flow measurements of approach-to-equilibrium changes in intrinsic protein fluorescence indicated that the Type I and Type II metals bind in different modes that induce distinct conformational effects on PAI-1. Changes in the observed rate constants with varying concentrations of metal allowed accurate determination of binding affinities for cobalt, nickel, and copper, yielding dissociation constants of ∼40, 30, and 0.09 μM, respectively. Competition experiments that tested effects on PAI-1 stability were consistent with these measurements of affinity and indicate that copper binds tightly to PAI-1.
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