1bml

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(New page: 200px<br /> <applet load="1bml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bml, resolution 2.9&Aring;" /> '''COMPLEX OF THE CATAL...)
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caption="1bml, resolution 2.9&Aring;" />
'''COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE'''<br />
'''COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE'''<br />
==Overview==
==Overview==
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Streptokinase is a plasminogen activator widely used in treating, blood-clotting disorders. Complexes of streptokinase with human, plasminogen can hydrolytically activate other plasminogen molecules to, plasmin, which then dissolves blood clots. A similar binding activation, mechanism also occurs in some key steps of blood coagulation. The crystal, structure of streptokinase complexed with the catalytic unit of human, plasmin was solved at 2.9 angstroms. The amino-terminal domain of, streptokinase in the complex is hypothesized to enhance the substrate, recognition. The carboxyl-terminal domain of streptokinase, which binds, near the activation loop of plasminogen, is likely responsible for the, contact activation of plasminogen in the complex.
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Streptokinase is a plasminogen activator widely used in treating blood-clotting disorders. Complexes of streptokinase with human plasminogen can hydrolytically activate other plasminogen molecules to plasmin, which then dissolves blood clots. A similar binding activation mechanism also occurs in some key steps of blood coagulation. The crystal structure of streptokinase complexed with the catalytic unit of human plasmin was solved at 2.9 angstroms. The amino-terminal domain of streptokinase in the complex is hypothesized to enhance the substrate recognition. The carboxyl-terminal domain of streptokinase, which binds near the activation loop of plasminogen, is likely responsible for the contact activation of plasminogen in the complex.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1BML is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Streptococcus_dysgalactiae_subsp._equisimilis Streptococcus dysgalactiae subsp. equisimilis]. Active as [http://en.wikipedia.org/wiki/Plasmin Plasmin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.7 3.4.21.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BML OCA].
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1BML is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Streptococcus_dysgalactiae_subsp._equisimilis Streptococcus dysgalactiae subsp. equisimilis]. Active as [http://en.wikipedia.org/wiki/Plasmin Plasmin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.7 3.4.21.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BML OCA].
==Reference==
==Reference==
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[[Category: Streptococcus dysgalactiae subsp. equisimilis]]
[[Category: Streptococcus dysgalactiae subsp. equisimilis]]
[[Category: Wang, X.]]
[[Category: Wang, X.]]
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[[Category: Zhang, X.C.]]
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[[Category: Zhang, X C.]]
[[Category: human plasmin]]
[[Category: human plasmin]]
[[Category: streptokinase]]
[[Category: streptokinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:11:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:50 2008''

Revision as of 09:56, 21 February 2008


1bml, resolution 2.9Å

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COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE

Contents

Overview

Streptokinase is a plasminogen activator widely used in treating blood-clotting disorders. Complexes of streptokinase with human plasminogen can hydrolytically activate other plasminogen molecules to plasmin, which then dissolves blood clots. A similar binding activation mechanism also occurs in some key steps of blood coagulation. The crystal structure of streptokinase complexed with the catalytic unit of human plasmin was solved at 2.9 angstroms. The amino-terminal domain of streptokinase in the complex is hypothesized to enhance the substrate recognition. The carboxyl-terminal domain of streptokinase, which binds near the activation loop of plasminogen, is likely responsible for the contact activation of plasminogen in the complex.

Disease

Known diseases associated with this structure: Conjunctivitis, ligneous OMIM:[173350], Plasminogen Tochigi disease OMIM:[173350], Plasminogen deficiency, types I and II OMIM:[173350], Thrombophilia, dysplasminogenemic OMIM:[173350]

About this Structure

1BML is a Protein complex structure of sequences from Homo sapiens and Streptococcus dysgalactiae subsp. equisimilis. Active as Plasmin, with EC number 3.4.21.7 Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic domain of human plasmin complexed with streptokinase., Wang X, Lin X, Loy JA, Tang J, Zhang XC, Science. 1998 Sep 11;281(5383):1662-5. PMID:9733510

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