1rjx: Difference between revisions
New page: left|200px<br /> <applet load="1rjx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rjx, resolution 2.3Å" /> '''Human PLASMINOGEN CA... |
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'''Human PLASMINOGEN CATALYTIC DOMAIN, K698M MUTANT'''<br /> | '''Human PLASMINOGEN CATALYTIC DOMAIN, K698M MUTANT'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1RJX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | 1RJX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1RJX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: streptokinase]] | [[Category: streptokinase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:48:44 2008'' | ||
Revision as of 14:48, 15 February 2008
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Human PLASMINOGEN CATALYTIC DOMAIN, K698M MUTANT
Overview
Streptokinase (SK) is a human plasminogen (Pg) activator secreted by, streptococci. The activation mechanism of SK differs from that of, physiological Pg activators in that SK is not a protease and cannot, proteolytically activate Pg. Instead, it forms a tight complex with Pg, that proteolytically activates other Pg molecules. The residue Lys-698 of, human Pg was hypothesized to participate in triggering activation in the, SK-Pg complex. Here, we report a study of the Lys-698 to Met substitution, in the catalytic domain of Pg (microPg) containing the proteolytic, activation-resistant background (R561A). While it remains competent in, forming a complex with SK, maintaining a comparable equilibration, dissociation constant (K(D)), the recombinant protein shows a nearly, 60-fold reduction in amidolytic activity relative to its R561A background, when mixed with native SK. A 2.3 A crystal structure of this mutant, microPg confirmed the correct folding of this recombinant protein., Combined with other biochemical data, these results support the premise, that Lys-698 of human Pg plays a functional role in the so-called, N-terminal insertion activation mechanism by SK.
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
1RJX is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Active as Plasmin, with EC number 3.4.21.7 Full crystallographic information is available from OCA.
Reference
Characterization of Lys-698-to-Met substitution in human plasminogen catalytic domain., Terzyan S, Wakeham N, Zhai P, Rodgers K, Zhang XC, Proteins. 2004 Aug 1;56(2):277-84. PMID:15211511
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