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9pai
From Proteopedia
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(New page: 200px<br /> <applet load="9pai" size="450" color="white" frame="true" align="right" spinBox="true" caption="9pai, resolution 2.7Å" /> '''CLEAVED SUBSTRATE VA...)
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Revision as of 21:51, 12 November 2007
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CLEAVED SUBSTRATE VARIANT OF PLASMINOGEN ACTIVATOR INHIBITOR-1
Contents |
Overview
Plasminogen activator inhibitor-1 (PAI-1) is unique among the serine, proteinase inhibitors (serpins) in that it can adopt at least three, different conformations (active, substrate and latent). We report the, X-ray structure of a cleaved substrate variant of human PAI-1, which has a, new beta-strand s4A formed by insertion of the amino-terminal portion of, the reactive-site loop into beta-sheet A subsequent to cleavage. This is, in contrast to the previous suggestion that the non-inhibitory function of, substrate-type serpins is mainly due to an inability of the reactive-site, loop to adopt this conformation. Comparison with the structure of latent, PAI-1 provides insights into the molecular determinants responsible for, the transition of the stressed active conformation to the thermostable, latent conformation.
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
9PAI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1., Aertgeerts K, De Bondt HL, De Ranter CJ, Declerck PJ, Nat Struct Biol. 1995 Oct;2(10):891-7. PMID:7552714
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