1fmg
From Proteopedia
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- | [[Image:1fmg.gif|left|200px]] | + | [[Image:1fmg.gif|left|200px]] |
- | + | ||
- | '''CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL''' | + | {{Structure |
+ | |PDB= 1fmg |SIZE=350|CAPTION= <scene name='initialview01'>1fmg</scene>, resolution 1.9Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1FMG is a [ | + | 1FMG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMG OCA]. |
==Reference== | ==Reference== | ||
- | Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol., Deepthi S, Johnson A, Pattabhi V, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1506-12. Epub 2001, Oct 25. PMID:[http:// | + | Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol., Deepthi S, Johnson A, Pattabhi V, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1506-12. Epub 2001, Oct 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11679713 11679713] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:02 2008'' |
Revision as of 09:11, 20 March 2008
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, resolution 1.9Å | |||||||
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Ligands: | , and | ||||||
Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL
Overview
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.
About this Structure
1FMG is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol., Deepthi S, Johnson A, Pattabhi V, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1506-12. Epub 2001, Oct 25. PMID:11679713
Page seeded by OCA on Thu Mar 20 11:11:02 2008
Categories: Single protein | Sus scrofa | Trypsin | Deepthi, S. | Johnson, A. | Pattabhi, V. | CA | EDO | SO4 | Hydrolase | Serine protease