9pai
From Proteopedia
(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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| - | [[Image:9pai.gif|left|200px]]<br /> | + | [[Image:9pai.gif|left|200px]]<br /><applet load="9pai" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="9pai" size=" | + | |
caption="9pai, resolution 2.7Å" /> | caption="9pai, resolution 2.7Å" /> | ||
'''CLEAVED SUBSTRATE VARIANT OF PLASMINOGEN ACTIVATOR INHIBITOR-1'''<br /> | '''CLEAVED SUBSTRATE VARIANT OF PLASMINOGEN ACTIVATOR INHIBITOR-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Plasminogen activator inhibitor-1 (PAI-1) is unique among the serine | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 9PAI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 9PAI is a [http://en.wikipedia.org/wiki/Single_protein 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=9PAI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aertgeerts, K.]] | [[Category: Aertgeerts, K.]] | ||
| - | [[Category: Bondt, H | + | [[Category: Bondt, H L.De.]] |
| - | [[Category: Declerck, P | + | [[Category: Declerck, P J.]] |
| - | [[Category: Ranter, C | + | [[Category: Ranter, C J.De.]] |
[[Category: serpin]] | [[Category: serpin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:18:51 2008'' |
Revision as of 17:18, 21 February 2008
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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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