1dvm

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Revision as of 17:30, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1dvm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dvm, resolution 2.40Å" /> '''ACTIVE FORM OF HUMA...)
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File:1dvm.gif


1dvm, resolution 2.40Å

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ACTIVE FORM OF HUMAN PAI-1

OverviewOverview

Serpins exhibit a range of physiological roles and can contribute to, certain disease states dependent on their various conformations., Understanding the mechanisms of the large-scale conformational, reorganizations of serpins may lead to a better understanding of their, roles in various cardiovascular diseases. We have studied the serpin, plasminogen activator inhibitor 1 (PAI-1), in both the active and the, latent state and found that anionic halide ions may play a role in the, active-to-latent structural transition. Crystallographic analysis of a, stable mutant form of active PAI-1 identified an anion-binding site, between the central beta-sheet and a small surface domain. A chloride ion, was modeled in this site, and its identity was confirmed by soaking, crystals in a bromide-containing solution and calculating a, crystallographic difference map. The anion thus located forms a 4-fold, ligated linchpin that tethers the surface domain to the central beta-sheet, into which the reactive center loop must insert during the, active-to-latent transition. Timecourse experiments measuring active PAI-1, stability in the presence of various halide ions showed a clear trend for, stabilization of the active form with F(-) > Cl(-) > Br(-) >> I(-). We, propose that the "stickiness" of this pin (i.e., the electronegativity of, the anion) contributes to the energetics of the active-to-latent, transition in the PAI-1 serpin.

DiseaseDisease

Known diseases associated with this structure: Hemorrhagic diathesis due to PAI1 deficiency OMIM:[173360], Thrombophilia due to excessive plasminogen activator inhibitor OMIM:[173360]

About this StructureAbout this Structure

1DVM is a Single protein structure of sequence from Homo sapiens with CL as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structures of active and latent PAI-1: a possible stabilizing role for chloride ions., Stout TJ, Graham H, Buckley DI, Matthews DJ, Biochemistry. 2000 Jul 25;39(29):8460-9. PMID:10913251

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