1FNI

CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.01% POLYDOCANOL

Summary for 1FNI

• Entry DOI: 10.2210/pdb1fni/pdb
• Related: 1FMG 1FN6 1QQU
• Descriptor: TRYPSIN, SULFATE ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: serine protease, hydrolase
• Biological source: Sus scrofa (pig)
• Cellular location: Secreted, extracellular space: P00761
• Total number of polymer chains: 1
• Total formula weight: 23875.94

Authors

Deepthi, S.,Johnson, A.,Pattabhi, V. (deposition date: 2000-08-22, release date: 2000-09-13, Last modification date: 2024-10-30)

Primary citation

Deepthi, S.,Johnson, A.,Pattabhi, V.
Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol.
Acta Crystallogr.,Sect.D, 57:1506-1512, 2001

PubMed Abstract: Polydocanol has a wide range of medical applications, especially in sclerotherapy of many diseases such as gastrointestinal antiplastia, oesophageal haemangioma etc. It is of interest to study the mode of binding of this medically important detergent and its subsequent action on proteins. Here, three crystal structures of serine protease trypsin are reported in the presence of varying concentrations of polydocanol in order to elucidate its mode of binding and interactions with proteins. Polydocanol binds to the protein with its hydrophilic head rather than the hydrophobic tail as is the case with other detergents such as SDS and MEGA-8. This hydrophilic binding mode results in the binding sites of polydocanol being distributed on the surface of the enzyme. There are at least 11 binding sites for polydocanol in trypsin. Polydocanol forms part of the large-scale water networks which connect distant regions of the enzyme, thereby stabilizing it. The hydrophilic binding of polydocanol also results in cross-linked pairs of trypsin molecules.

PubMed: 11679713
DOI: 10.1107/S0907444901011143

Experimental method

X-RAY DIFFRACTION (1.6 Å)