1YF4

Crystal Structure of trypsin-vasopressin complex

Summary for 1YF4

• Entry DOI: 10.2210/pdb1yf4/pdb
• Descriptor: Trypsin, Vasopressin, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: trypsin, vasopressin, peptide binding, hydrolase-hormone-growth factor complex, hydrolase/hormone/growth factor
• Biological source: Sus scrofa (pig); More
• Cellular location: Secreted, extracellular space: P00761
• Total number of polymer chains: 2
• Total formula weight: 24619.82

Authors

Syed Ibrahim, B.,Pattabhi, V. (deposition date: 2004-12-30, release date: 2005-05-24, Last modification date: 2024-10-30)

Primary citation

Syed Ibrahim, B.,Pattabhi, V.
Trypsin inhibition by a Peptide hormone: crystal structure of trypsin-vasopressin complex
J.Mol.Biol., 348:1191-1198, 2005

PubMed Abstract: 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.

PubMed: 15854654
DOI: 10.1016/j.jmb.2005.03.034

Experimental method

X-RAY DIFFRACTION (1.98 Å)