1dm4

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[[Image:1dm4.gif|left|200px]]<br /><applet load="1dm4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dm4.gif|left|200px]]
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caption="1dm4, resolution 2.50&Aring;" />
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'''SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)'''<br />
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{{Structure
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|PDB= 1dm4 |SIZE=350|CAPTION= <scene name='initialview01'>1dm4</scene>, resolution 2.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DM4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DM4 OCA].
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1DM4 is a [[Protein complex]] structure of sequences 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=1DM4 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10739913 10739913]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10739913 10739913]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Tulinsky, A.]]
[[Category: Tulinsky, A.]]
[[Category: ACE]]
[[Category: ACE]]
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[[Category: fibrinopeptide a]]
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[[Category: fibrinopeptide some]]
[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: mutant thrombin]]
[[Category: mutant thrombin]]
[[Category: residual catalytic activity]]
[[Category: residual catalytic activity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:40:38 2008''

Revision as of 08:40, 20 March 2008


PDB ID 1dm4

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, resolution 2.50Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)


Contents

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.

Disease

Known diseases associated with this structure: Dysprothrombinemia OMIM:[176930], Hyperprothrombinemia OMIM:[176930], Hypoprothrombinemia OMIM:[176930]

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

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