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9pai

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(New page: 200px<br /> <applet load="9pai" size="450" color="white" frame="true" align="right" spinBox="true" caption="9pai, resolution 2.7&Aring;" /> '''CLEAVED SUBSTRATE VA...)
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[[Image:9pai.gif|left|200px]]<br /><applet load="9pai" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="9pai" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="9pai, resolution 2.7&Aring;" />
caption="9pai, resolution 2.7&Aring;" />
'''CLEAVED SUBSTRATE VARIANT OF PLASMINOGEN ACTIVATOR INHIBITOR-1'''<br />
'''CLEAVED SUBSTRATE VARIANT OF PLASMINOGEN ACTIVATOR INHIBITOR-1'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=9PAI OCA].
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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.]]
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[[Category: Bondt, H.L.De.]]
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[[Category: Bondt, H L.De.]]
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[[Category: Declerck, P.J.]]
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[[Category: Declerck, P J.]]
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[[Category: Ranter, C.J.De.]]
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[[Category: Ranter, C J.De.]]
[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:57:35 2007''
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''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


9pai, resolution 2.7Å

Drag the structure with the mouse to rotate

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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