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| | <StructureSection load='3aav' size='340' side='right'caption='[[3aav]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3aav' size='340' side='right'caption='[[3aav]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3aav]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3AAV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3aav]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2C:3,3-[ETHANE-1,2-DIYLBIS(NITRILOMETHYLYLIDENE)]BIS(4-HYDROXYBENZENECARBOXIMIDAMIDE)'>A2C</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aas|3aas]], [[3aau|3aau]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2C:3,3-[ETHANE-1,2-DIYLBIS(NITRILOMETHYLYLIDENE)]BIS(4-HYDROXYBENZENECARBOXIMIDAMIDE)'>A2C</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=3aav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aav OCA], [https://pdbe.org/3aav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aav RCSB], [https://www.ebi.ac.uk/pdbsum/3aav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aav ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3aav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aav OCA], [http://pdbe.org/3aav PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aav RCSB], [http://www.ebi.ac.uk/pdbsum/3aav PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aav ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trypsin]]
| + | [[Category: Iyaguchi D]] |
| - | [[Category: Iyaguchi, D]] | + | [[Category: Kawano S]] |
| - | [[Category: Kawano, S]] | + | [[Category: Toyota E]] |
| - | [[Category: Toyota, E]] | + | |
| - | [[Category: Calcium]]
| + | |
| - | [[Category: Coordination metal based inhibitor]]
| + | |
| - | [[Category: Digestion]]
| + | |
| - | [[Category: Enzyme-inhibitor complex]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| - | [[Category: Zymogen]]
| + | |
| Structural highlights
Function
TRY1_BOVIN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structures of the complexes of bovine trypsin with m-guanidinosalicylidene-l-alaninato(aqua)copper(II) hydrochloride (inhibitor 1), [N,N'-bis(m-guanidinosalicylidene)ethylenediaminato]copper(II) (inhibitor 2), and [N,N'-bis(m-amidinosalicylidene)ethylenediaminato]copper(II) (inhibitor 4) have been determined. The guanidine-containing trypsin-inhibitors (1 and 2) bind to the trypsin active site in a manner similar to that previously reported for amidine-containing inhibitors, for example, m-amidinosalicylidene-l-alaninato(aqua)copper(II) hydrochloride (inhibitor 3). However, the binding mode of the guanidino groups of inhibitors 1 and 2 to Asp189 in the S1 pocket of trypsin was found to be markedly different from that of the amidino group of inhibitor 3. The present X-ray analyses revealed that the interactions of the metal ion of the inhibitors with the active site residues of trypsin play a crucial role in the binding affinity to the trypsin molecule. These structural information and inhibitory activity data for amidine- and guanidine-containing Schiff base metal chelate inhibitors provide new avenues for designing novel inhibitors against physiologically important trypsin-like serine proteases.
Structural basis for the design of novel Schiff base metal chelate inhibitors of trypsin.,Iyaguchi D, Kawano S, Takada K, Toyota E Bioorg Med Chem. 2010 Mar 15;18(6):2076-80. Epub 2010 Feb 15. PMID:20202854[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Iyaguchi D, Kawano S, Takada K, Toyota E. Structural basis for the design of novel Schiff base metal chelate inhibitors of trypsin. Bioorg Med Chem. 2010 Mar 15;18(6):2076-80. Epub 2010 Feb 15. PMID:20202854 doi:10.1016/j.bmc.2010.02.016
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