1fmg: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL== | ==CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL== | ||
<StructureSection load='1fmg' size='340' side='right' caption='[[1fmg]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1fmg' size='340' side='right'caption='[[1fmg]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fmg]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1fmg]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
< | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmg OCA], [https://pdbe.org/1fmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmg RCSB], [https://www.ebi.ac.uk/pdbsum/1fmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmg ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRYP_PIG TRYP_PIG] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 14: | Line 15: | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fmg_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fmg_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 30: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[Carbonic anhydrase|Carbonic anhydrase]] | *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]] | ||
*[[Trypsin|Trypsin]] | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Deepthi S]] | |||
[[Category: Deepthi | [[Category: Johnson A]] | ||
[[Category: Johnson | [[Category: Pattabhi V]] | ||
[[Category: Pattabhi | |||
Latest revision as of 12:36, 25 December 2024
CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOLCRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPolydocanol 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||