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1tmu

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[[Image:1tmu.gif|left|200px]]
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{{STRUCTURE_1tmu| PDB=1tmu | SCENE= }}
{{STRUCTURE_1tmu| PDB=1tmu | SCENE= }}
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'''CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS'''
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===CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS===
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==Overview==
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The three-dimensional structures of D-Phe-Pro-Arg-chloromethyl ketone-inhibited thrombin in complex with Tyr-63-sulfated hirudin (ternary complex) and of thrombin in complex with the bifunctional inhibitor D-Phe-Pro-Arg-Pro-(Gly)4-hirudin (CGP 50,856, binary complex) have been determined by X-ray crystallography in crystal forms different from those described by Skrzypczak-Jankun et al. (Skrzypczak-Jankun, E., Carperos, V.E., Ravichandran, K.G., &amp; Tulinsky, A., 1991, J. Mol. Biol. 221, 1379-1393). In both complexes, the interactions of the C-terminal hirudin segments of the inhibitors binding to the fibrinogen-binding exosite of thrombin are clearly established, including residues 60-64, which are disordered in the earlier crystal form. The interactions of the sulfate group of Tyr-63 in the ternary complex structure explain why natural sulfated hirudin binds with a 10-fold lower K(i) than the desulfated recombinant material. In this new crystal form, the autolysis loop of thrombin (residues 146-150), which is disordered in the earlier crystal form, is ordered due to crystal contacts. Interactions between the C-terminal fragment of hirudin and thrombin are not influenced by crystal contacts in this new crystal form, in contrast to the earlier form. In the bifunctional inhibitor-thrombin complex, the peptide bond between Arg-Pro (P1-P1') seems to be cleaved.
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{{ABSTRACT_PUBMED_8251938}}
==About this Structure==
==About this Structure==
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[[Category: Gruetter, M G.]]
[[Category: Gruetter, M G.]]
[[Category: Priestle, J P.]]
[[Category: Priestle, J P.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:22:31 2008''

Revision as of 14:22, 27 July 2008

Image:1tmu.png

Template:STRUCTURE 1tmu

CHANGES IN INTERACTIONS IN COMPLEXES OF HIRUDIN DERIVATIVES AND HUMAN ALPHA-THROMBIN DUE TO DIFFERENT CRYSTAL FORMS

Template:ABSTRACT PUBMED 8251938

About this Structure

1TMU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms., Priestle JP, Rahuel J, Rink H, Tones M, Grutter MG, Protein Sci. 1993 Oct;2(10):1630-42. PMID:8251938

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