1FMG: CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL

Citation:
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.
PDB ID: 1FMGDownload
MMDB ID: 14426
PDB Deposition Date: 2000/8/17
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1FMG: monomeric; determined by author
Molecular Components in 1FMG
Label Count Molecule
Protein (1 molecule)
1
Trypsin
Molecule annotation
Chemicals (7 molecules)
1
1
2
1
3
5
* Click molecule labels to explore molecular sequence information.

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