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1brb

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(New page: 200px<br /><applet load="1brb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1brb, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURES OF...)
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[[Image:1brb.gif|left|200px]]<br /><applet load="1brb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1brb, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI==
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The crystal structure of rat anionic trypsin D189G/G226D has been, determined in complexes with each of the protein inhibitors APPI (amyloid, beta-protein precursor inhibitor domain) and BPTI (bovine pancreatic, trypsin inhibitor) at resolutions of 2.5 A and 2.1 A, respectively., Comparisons with the structure of the bovine trypsin-BPTI complex show, that the enzyme-inhibitor interactions in rat trypsin are dominated to a, much greater degree by attractive and repulsive electrostatic forces., Decreased structural complementarity in the flanking regions of the, interface formed with BPTI is reflected in significantly weaker inhibition, relative to bovine trypsin. The primary active site loop of BPTI adopts, slightly different conformations when bound to rat and cow trypsins, reflecting a broader entrance to the binding pocket in the former. Tight, complementarity of each loop conformer to the respective active sites then, gives rise to significantly different overall orientations of the, inhibitor when bound to the two enzymes. The crystal structures of trypsin, bound to these protein inhibitors are excellent models of the Michaelis, complexes, which permit visualization of substrate interactions both N and, C-terminal to the cleaved bond, while maintaining identical reaction, chemistry. They will be uniquely useful to the structure-function analysis, of variant rat trypsin enzymes.
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<StructureSection load='1brb' size='340' side='right'caption='[[1brb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1brb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRB FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1brb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brb OCA], [https://pdbe.org/1brb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1brb RCSB], [https://www.ebi.ac.uk/pdbsum/1brb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1brb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRY2_RAT TRY2_RAT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1brb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1brb ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BRB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BRB OCA].
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*[[BPTI 3D structures|BPTI 3D structures]]
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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==Reference==
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__TOC__
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Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI., Perona JJ, Tsu CA, Craik CS, Fletterick RJ, J Mol Biol. 1993 Apr 5;230(3):919-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7683059 7683059]
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</StructureSection>
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[[Category: Protein complex]]
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Trypsin]]
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[[Category: Fletterick RJ]]
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[[Category: Fletterick, R.J.]]
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[[Category: Perona JJ]]
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[[Category: Perona, J.J.]]
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[[Category: complex(proteinase/inhibitor)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:51:16 2007''
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Current revision

CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI

PDB ID 1brb

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