1dvm

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[[Image:1dvm.gif|left|200px]]
[[Image:1dvm.gif|left|200px]]
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{{Structure
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|PDB= 1dvm |SIZE=350|CAPTION= <scene name='initialview01'>1dvm</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_1dvm", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= UMBILICAL VEIN ENDOTHELIUM LIBRARY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1dvm| PDB=1dvm | SCENE= }}
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|RELATEDENTRY=[[1a7c|1A7C]], [[1b3k|1B3K]], [[1c5g|1C5G]], [[1db2|1DB2]], [[1dvn|1DVN]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvm OCA], [http://www.ebi.ac.uk/pdbsum/1dvm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dvm RCSB]</span>
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}}
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'''ACTIVE FORM OF HUMAN PAI-1'''
'''ACTIVE FORM OF HUMAN PAI-1'''
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[[Category: Matthews, D J.]]
[[Category: Matthews, D J.]]
[[Category: Stout, T J.]]
[[Category: Stout, T J.]]
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[[Category: inhibitor]]
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[[Category: Inhibitor]]
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[[Category: pai-1]]
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[[Category: Pai-1]]
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[[Category: serpin]]
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[[Category: Serpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:20:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:49:39 2008''
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Revision as of 11:20, 2 May 2008

Image:1dvm.gif

Template:STRUCTURE 1dvm

ACTIVE FORM OF HUMAN PAI-1


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.

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 Fri May 2 14:20:09 2008

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