1dm4
From Proteopedia
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|PDB= 1dm4 |SIZE=350|CAPTION= <scene name='initialview01'>1dm4</scene>, resolution 2.50Å | |PDB= 1dm4 |SIZE=350|CAPTION= <scene name='initialview01'>1dm4</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dm4 OCA], [http://www.ebi.ac.uk/pdbsum/1dm4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dm4 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The Ser195Ala mutant of human alpha-thrombin was complexed with fibrinopeptide A(7-22) (FPA) in an effort to describe the (P1'-P6') post-cleavage binding subsites of the fibrinogen-recognition exosite and define more clearly the nature of the Michaelis complex and the scissile peptide bond bound at the catalytic site. The thrombin mutant, however, has residual catalytic activity and proteolysis occurred at the Arg16-Gly17 bond. Thus, the structure of the thrombin complex determined was that of FPA(7-16) bound at the active site, which is very similar to the ternary FPA(7-16)cmk-human thrombin-hirugen complex (r.m.s.d. approximately 0.4 A; Stubbs et al. , 1992). It is further shown by subsidiary experiments that the cleavage is the result of residual catalytic activity of the altered catalytic machinery. | The Ser195Ala mutant of human alpha-thrombin was complexed with fibrinopeptide A(7-22) (FPA) in an effort to describe the (P1'-P6') post-cleavage binding subsites of the fibrinogen-recognition exosite and define more clearly the nature of the Michaelis complex and the scissile peptide bond bound at the catalytic site. The thrombin mutant, however, has residual catalytic activity and proteolysis occurred at the Arg16-Gly17 bond. Thus, the structure of the thrombin complex determined was that of FPA(7-16) bound at the active site, which is very similar to the ternary FPA(7-16)cmk-human thrombin-hirugen complex (r.m.s.d. approximately 0.4 A; Stubbs et al. , 1992). It is further shown by subsidiary experiments that the cleavage is the result of residual catalytic activity of the altered catalytic machinery. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Dysprothrombinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176930 176930]], Hyperprothrombinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176930 176930]], Hypoprothrombinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176930 176930]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Sadler, E J.]] | [[Category: Sadler, E J.]] | ||
[[Category: Tulinsky, A.]] | [[Category: Tulinsky, A.]] | ||
| - | [[Category: ACE]] | ||
[[Category: fibrinopeptide some]] | [[Category: fibrinopeptide some]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: residual catalytic activity]] | [[Category: residual catalytic activity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:44:10 2008'' |
Revision as of 16:44, 30 March 2008
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| , resolution 2.50Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)
Overview
The Ser195Ala mutant of human alpha-thrombin was complexed with fibrinopeptide A(7-22) (FPA) in an effort to describe the (P1'-P6') post-cleavage binding subsites of the fibrinogen-recognition exosite and define more clearly the nature of the Michaelis complex and the scissile peptide bond bound at the catalytic site. The thrombin mutant, however, has residual catalytic activity and proteolysis occurred at the Arg16-Gly17 bond. Thus, the structure of the thrombin complex determined was that of FPA(7-16) bound at the active site, which is very similar to the ternary FPA(7-16)cmk-human thrombin-hirugen complex (r.m.s.d. approximately 0.4 A; Stubbs et al. , 1992). It is further shown by subsidiary experiments that the cleavage is the result of residual catalytic activity of the altered catalytic machinery.
About this Structure
1DM4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the Ser195Ala mutant of human alpha--thrombin complexed with fibrinopeptide A(7--16): evidence for residual catalytic activity., Krishnan R, Sadler JE, Tulinsky A, Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):406-10. PMID:10739913
Page seeded by OCA on Sun Mar 30 19:44:10 2008
