1tpg
From Proteopedia
(New page: 200px<br /> <applet load="1tpg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tpg" /> '''F1-G MODULE PAIR RESIDUES 1-91 (C83S) OF TI...) |
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'''F1-G MODULE PAIR RESIDUES 1-91 (C83S) OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (T-PA) (NMR, 298K, PH2.95, REPRESENTATIVE STRUCTURE)'''<br /> | '''F1-G MODULE PAIR RESIDUES 1-91 (C83S) OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (T-PA) (NMR, 298K, PH2.95, REPRESENTATIVE STRUCTURE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The thrombolytic serine protease tissue-type plasminogen | + | BACKGROUND: The thrombolytic serine protease tissue-type plasminogen activator (t-PA) is a classical modular protein consisting of three types of domain in addition to the serine protease domain: F1 (homologous to fibronectin type I); G (epidermal growth factor-like) and kringle. Biochemical data suggest that the F1 and G modules play a major role in the binding of t-PA to fibrin and to receptors on hepatocytes. RESULTS: We have derived the solution structure of the F1 and G pair of modules from t-PA by two- and three-dimensional NMR techniques, in combination with dynamical simulated annealing calculations. We have also obtained information about the molecule's backbone dynamics through measurement of amide 15N relaxation parameters. CONCLUSIONS: Although the F1 and G modules each adopt their expected tertiary structure, the modules interact intimately to bury a hydrophobic core, and the inter-module linker makes up the third strand of the G module's major beta-sheet. The new structural results allow the interpretation of earlier mutational data relevant to fibrin-binding and hepatocyte-receptor binding. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/T-plasminogen_activator T-plasminogen activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.68 3.4.21.68] Full crystallographic information is available from [http:// | + | 1TPG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/T-plasminogen_activator T-plasminogen activator], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.68 3.4.21.68] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: T-plasminogen activator]] | [[Category: T-plasminogen activator]] | ||
| - | [[Category: Campbell, I | + | [[Category: Campbell, I D.]] |
| - | [[Category: Downing, A | + | [[Category: Downing, A K.]] |
| - | [[Category: Driscoll, P | + | [[Category: Driscoll, P C.]] |
| - | [[Category: Dudgeon, T | + | [[Category: Dudgeon, T J.]] |
| - | [[Category: Smith, B | + | [[Category: Smith, B O.]] |
[[Category: plasminogen activation]] | [[Category: plasminogen activation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:59 2008'' |
Revision as of 13:16, 21 February 2008
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F1-G MODULE PAIR RESIDUES 1-91 (C83S) OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (T-PA) (NMR, 298K, PH2.95, REPRESENTATIVE STRUCTURE)
Contents |
Overview
BACKGROUND: The thrombolytic serine protease tissue-type plasminogen activator (t-PA) is a classical modular protein consisting of three types of domain in addition to the serine protease domain: F1 (homologous to fibronectin type I); G (epidermal growth factor-like) and kringle. Biochemical data suggest that the F1 and G modules play a major role in the binding of t-PA to fibrin and to receptors on hepatocytes. RESULTS: We have derived the solution structure of the F1 and G pair of modules from t-PA by two- and three-dimensional NMR techniques, in combination with dynamical simulated annealing calculations. We have also obtained information about the molecule's backbone dynamics through measurement of amide 15N relaxation parameters. CONCLUSIONS: Although the F1 and G modules each adopt their expected tertiary structure, the modules interact intimately to bury a hydrophobic core, and the inter-module linker makes up the third strand of the G module's major beta-sheet. The new structural results allow the interpretation of earlier mutational data relevant to fibrin-binding and hepatocyte-receptor binding.
Disease
Known disease associated with this structure: Plasminogen activator deficiency OMIM:[173370]
About this Structure
1TPG is a Single protein structure of sequence from Homo sapiens. Active as T-plasminogen activator, with EC number 3.4.21.68 Full crystallographic information is available from OCA.
Reference
The solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator., Smith BO, Downing AK, Driscoll PC, Dudgeon TJ, Campbell ID, Structure. 1995 Aug 15;3(8):823-33. PMID:7582899
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