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| - | [[Image:1hgt.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1hgt| PDB=1hgt | SCENE= }} | | {{STRUCTURE_1hgt| PDB=1hgt | SCENE= }} |
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| - | '''STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN'''
| + | ===STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN=== |
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| - | ==Overview==
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| - | The isomorphous structures of the hirugen (N-acetylhirudin 53'-64' with sulfato-Tyr63') and hirulog 1 (D-Phe-Pro-Arg-Pro-(Gly)4 desulfato-Tyr63'-hirugen) complexes of human alpha-thrombin have been determined and refined at 2.2 A resolution to crystallographic R-factors of 0.167 and 0.163, respectively. The binding of hirugen to thrombin is similar to that of the binding of the C-terminal dodecapeptide of hirudin, including that of the terminal 3(10) helical turn. The sulfato Tyr63', which, as a result of sulfation, increases the binding affinity by an order of magnitude, is involved in an extended hydrogen bonding network utilizing all three sulfato oxygen atoms. The hirugen-thrombin complex is the first thrombin structure determined to have an unobstructed active site; this site is practically identical in positioning of catalytic residues and in its hydrogen bonding pattern with that of other serine proteinases. Hirulog 1, which is a poor thrombin substrate, is cleaved at the Arg3'-Pro4' bond in the crystal structure. The Arg3' of hirulog 1 occupies the specificity site, the D-Phe-Pro-Arg tripeptide is positioned like that of D-Phe-Pro-Arg chloromethylketone in the active site and the Pro4'(Gly)4 spacer to hirugen is disordered in the structure, as is the 3(10) turn of hirugen. The latter must be related to the simultaneous absence both of sulfation and of the last residue of hirudin (Gln65'). In addition, the autolysis loop of thrombin (Lys145-Gly150) is disordered in both structures. Changes in circular dichroism upon hirugen binding are therefore most likely the result of the flexibility associated with this loop.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_1942057}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 1942057 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_1942057}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Skrzypczak-Jankun, E.]] | | [[Category: Skrzypczak-Jankun, E.]] |
| | [[Category: Tulinsky, A.]] | | [[Category: Tulinsky, A.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:49:48 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:09:54 2008'' |
Revision as of 05:09, 1 July 2008
Template:STRUCTURE 1hgt
STRUCTURE OF THE HIRUGEN AND HIRULOG 1 COMPLEXES OF ALPHA-THROMBIN
Template:ABSTRACT PUBMED 1942057
About this Structure
1HGT is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the hirugen and hirulog 1 complexes of alpha-thrombin., Skrzypczak-Jankun E, Carperos VE, Ravichandran KG, Tulinsky A, Westbrook M, Maraganore JM, J Mol Biol. 1991 Oct 20;221(4):1379-93. PMID:1942057
Page seeded by OCA on Tue Jul 1 08:09:54 2008
