1t7c

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(New page: 200px<br /><applet load="1t7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t7c, resolution 1.85&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1t7c.gif|left|200px]]<br /><applet load="1t7c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1t7c, resolution 1.85&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE P1 GLU BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE P1 GLU BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX==
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The bovine chymotrypsin-bovine pancreatic trypsin inhibitor (BPTI), interaction belongs to extensively studied models of protein-protein, recognition. The accommodation of the inhibitor P1 residue in the S1, binding site of the enzyme forms the hot spot of this interaction., Mutations introduced at the P1 position of BPTI result in a more than five, orders of magnitude difference of the association constant values with the, protease. To elucidate the structural aspects of the discrimination, between different P1 residues, crystal structures of five bovine, chymotrypsin-P1 BPTI variant complexes have been determined at pH 7.8 to a, resolution below 2 A. The set includes polar (Thr), ionizable (Glu, His), medium-sized aliphatic (Met) and large aromatic (Trp) P1 residues and, complements our earlier studies of the interaction of different P1, side-chains with the S1 pocket of chymotrypsin. The structures have been, compared to the complexes of proteases with similar and dissimilar P1, preferences, including Streptomyces griseus proteases B and E, human, neutrophil elastase, crab collagenase, bovine trypsin and human thrombin., The S1 sites of these enzymes share a common general shape of significant, rigidity. Large and branched P1 residues adapt in their complexes similar, conformations regardless of the polarity and size differences between, their S1 pockets. Conversely, long and flexible residues such as P1 Met, are present in the disordered form and display a conformational diversity, despite similar inhibitory properties with respect to most enzymes, studied. Thus, the S1 specificity profiles of the serine proteases appear, to result from the precise complementarity of the P1-S1 interface and, minor conformational adjustments occurring upon the inhibitor binding.
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<StructureSection load='1t7c' size='340' side='right'caption='[[1t7c]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1t7c]] is a 4 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=1T7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T7C 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]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1t7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7c OCA], [https://pdbe.org/1t7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t7c RCSB], [https://www.ebi.ac.uk/pdbsum/1t7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
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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/t7/1t7c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1t7c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The bovine chymotrypsin-bovine pancreatic trypsin inhibitor (BPTI) interaction belongs to extensively studied models of protein-protein recognition. The accommodation of the inhibitor P1 residue in the S1 binding site of the enzyme forms the hot spot of this interaction. Mutations introduced at the P1 position of BPTI result in a more than five orders of magnitude difference of the association constant values with the protease. To elucidate the structural aspects of the discrimination between different P1 residues, crystal structures of five bovine chymotrypsin-P1 BPTI variant complexes have been determined at pH 7.8 to a resolution below 2 A. The set includes polar (Thr), ionizable (Glu, His), medium-sized aliphatic (Met) and large aromatic (Trp) P1 residues and complements our earlier studies of the interaction of different P1 side-chains with the S1 pocket of chymotrypsin. The structures have been compared to the complexes of proteases with similar and dissimilar P1 preferences, including Streptomyces griseus proteases B and E, human neutrophil elastase, crab collagenase, bovine trypsin and human thrombin. The S1 sites of these enzymes share a common general shape of significant rigidity. Large and branched P1 residues adapt in their complexes similar conformations regardless of the polarity and size differences between their S1 pockets. Conversely, long and flexible residues such as P1 Met are present in the disordered form and display a conformational diversity despite similar inhibitory properties with respect to most enzymes studied. Thus, the S1 specificity profiles of the serine proteases appear to result from the precise complementarity of the P1-S1 interface and minor conformational adjustments occurring upon the inhibitor binding.
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==About this Structure==
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Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants.,Czapinska H, Helland R, Smalas AO, Otlewski J J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:15544809<ref>PMID:15544809</ref>
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1T7C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T7C OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants., Czapinska H, Helland R, Smalas AO, Otlewski J, J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15544809 15544809]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1t7c" style="background-color:#fffaf0;"></div>
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[[Category: Chymotrypsin]]
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[[Category: Protein complex]]
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[[Category: Czapinska, H.]]
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[[Category: Helland, R.]]
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[[Category: Otlewski, J.]]
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[[Category: Smalas, A.O.]]
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[[Category: SO4]]
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[[Category: chymotrypsin; serine proteinase; bovine pancreatic trypsin inhibitor; bpti; protein-protein interaction; non-cognate binding; s1 pocket; primary specificity; crystal structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:02:40 2007''
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==See Also==
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*[[BPTI 3D structures|BPTI 3D structures]]
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*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Czapinska H]]
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[[Category: Helland R]]
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[[Category: Otlewski J]]
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[[Category: Smalas AO]]

Current revision

CRYSTAL STRUCTURE OF THE P1 GLU BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX

PDB ID 1t7c

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