1bcu

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{{STRUCTURE_1bcu| PDB=1bcu | SCENE= }}
{{STRUCTURE_1bcu| PDB=1bcu | SCENE= }}
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'''ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND PROFLAVIN'''
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===ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND PROFLAVIN===
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==Overview==
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Proflavin can be used to study the interactions of inhibitors and substrates with thrombin by monitoring the changes in the visible absorption spectrum that occur on dye displacement. We have used microspectrophotometric methods to investigate the binding of proflavin to crystals of an alpha-thrombin-hirugen complex and have determined the structure by X-ray crystallography. The proflavin molecule binds in the S1 pocket of the enzyme with one of the amino groups hydrogen bonded to the carboxylate of Asp-189 while the protonated ring nitrogen is hydrogen bonded to the carbonyl of Gly-219. This result indicates that the proflavin displacement assay can be used to specifically monitor the binding of inhibitors to the S1 pocket.
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(as it appears on PubMed at http://www.pubmed.gov), where 9559654 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9559654}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:51:07 2008''

Revision as of 15:51, 30 June 2008

Image:1bcu.png

Template:STRUCTURE 1bcu

ALPHA-THROMBIN COMPLEXED WITH HIRUGEN AND PROFLAVIN

Template:ABSTRACT PUBMED 9559654

About this Structure

1BCU is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray and spectrophotometric studies of the binding of proflavin to the S1 specificity pocket of human alpha-thrombin., Conti E, Rivetti C, Wonacott A, Brick P, FEBS Lett. 1998 Mar 27;425(2):229-33. PMID:9559654

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