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PDBsum entry 3cvm
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Blood clotting
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PDB id
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3cvm
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References listed in PDB file
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Key reference
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Title
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High-Resolution structure of the stable plasminogen activator inhibitor type-1 variant 14-1b in its proteinase-Cleaved form: a new tool for detailed interaction studies and modeling.
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Authors
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J.K.Jensen,
P.G.Gettins.
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Ref.
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Protein Sci, 2008,
17,
1844-1849.
[DOI no: ]
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PubMed id
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Abstract
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Wild-type plasminogen activator inhibitor type-1 (PAI-1) rapidly converts to the
inactive latent state under conditions of physiological pH and temperature. For
in vivo studies of active PAI-1 in cell culture and in vivo model systems, the
14-1B PAI-1 mutant (N150H-K154T-Q319L-M354I), with its stabilized active
conformation, has thus become the PAI-1 of choice. As a consequence of the
increased stability, the only two forms likely to be encountered are the active
or the cleaved form, the latter either free or complexed with target proteinase.
We hereby report the first structure of the stable 14-1B PAI-1 variant in its
reactive center cleaved form, to a resolution of 2.0 A. The >99% complete
structure represents the highest resolved structure of free cleaved PAI-1. This
high-resolution structure should be of great use for drug target development and
for modeling protein-protein interactions such as those of PAI-1 with
vitronectin.
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Figure 3.
Figure 3. Close-up comparison of the ligand-binding cavity
in the flexible joints region of active 14-1B (1DVM) and rcc14-B
(3CVM, present structure). (A) Active 14-1B; (B) cleaved 14-1B.
The cavity boundaries are outlined by broken lines. Residues
surrounding the cavity are labeled.
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2008,
17,
1844-1849)
copyright 2008.
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