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| [[Image:1yf4.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1yf4| PDB=1yf4 | SCENE= }} | | {{STRUCTURE_1yf4| PDB=1yf4 | SCENE= }} |
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| '''Crystal Structure of trypsin-vasopressin complex'''
| | ===Crystal Structure of trypsin-vasopressin complex=== |
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| ==Overview==
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| The large variety of serine protease inhibitors, available from various sources such as tissues, microorganisms, plants, etc., play an important role in regulating the proteolytic enzymes. The analysis of protease-inhibitor complexes helps in understanding the mechanism of action, as well as in designing inhibitors. Vasopressin, an anti-diuretic nonapeptide hormone, is found to be an effective inhibitor of trypsin, with a K(i) value of 5 nM. The crystal structure of the trypsin-vasopressin complex revealed that vasopressin fulfils all the important interactions for an inhibitor, without any break in the scissile peptide bond. The cyclic nature due to a disulfide bridge between Cys1 and Cys6 of vasopressin provides structural rigidity to the peptide hormone. The trypsin-binding site is located at the C terminus, while the neurophysin-binding site is at the N terminus of vasopressin. This study will assist in designing new peptide inhibitors. This study suggests that vasopressin inhibition of trypsin may have unexplored biological implications. | | The line below this paragraph, {{ABSTRACT_PUBMED_15854654}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15854654 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15854654}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Trypsin]] | | [[Category: Trypsin]] |
| [[Category: Vasopressin]] | | [[Category: Vasopressin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:14:39 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:02:57 2008'' |
