1dvm
From Proteopedia
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- | [[Image:1dvm.gif|left|200px]] | + | [[Image:1dvm.gif|left|200px]] |
- | + | ||
- | '''ACTIVE FORM OF HUMAN PAI-1''' | + | {{Structure |
+ | |PDB= 1dvm |SIZE=350|CAPTION= <scene name='initialview01'>1dvm</scene>, resolution 2.40Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= UMBILICAL VEIN ENDOTHELIUM LIBRARY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''ACTIVE FORM OF HUMAN PAI-1''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1DVM is a [ | + | 1DVM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVM OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10913251 10913251] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serpin]] | [[Category: serpin]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:45:05 2008'' |
Revision as of 08:45, 20 March 2008
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, resolution 2.40Å | |||||||
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Ligands: | |||||||
Gene: | UMBILICAL VEIN ENDOTHELIUM LIBRARY (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
ACTIVE FORM OF HUMAN PAI-1
Contents |
Overview
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.
Disease
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 Structure
1DVM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 10:45:05 2008
Categories: Homo sapiens | Single protein | Buckley, D I. | Graham, H. | Matthews, D J. | Stout, T J. | CL | Inhibitor | Pai-1 | Serpin