3aav: Difference between revisions

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-{{Seed}}
-[[Image:3aav.jpg|left|200px]]
-<!--
+==Bovine beta-trypsin bound to meta-diamidino schiff base copper (II) chelate==
-The line below this paragraph, containing "STRUCTURE_3aav", creates the "Structure Box" on the page.
+<StructureSection load='3aav' size='340' side='right'caption='[[3aav]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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>
-{{STRUCTURE_3aav|  PDB=3aav  |  SCENE=  }}
+<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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/3aav_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3aav ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Bovine beta-trypsin bound to meta-diamidino schiff base copper (II) chelate===
+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<ref>PMID:20202854</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3aav" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20202854}}, adds the Publication Abstract to the page
+*[[Trypsin 3D structures|Trypsin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20202854 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20202854}}
+__TOC__
+</StructureSection>
-==About this Structure==
-AAV is a 2 chains structure with sequences 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].
-==Reference==
-<ref group="xtra">PMID:20202854</ref><references group="xtra"/>
 [[Category: Bos taurus]]
-[[Category: Trypsin]]
+[[Category: Large Structures]]
-[[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr  7 10:34:00 2010''