1ylc

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[[Image:1ylc.gif|left|200px]]<br /><applet load="1ylc" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ylc, resolution 1.70&Aring;" />
 
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'''Trypsin/BPTI complex mutant'''<br />
 
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==About this Structure==
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==Trypsin/BPTI complex mutant==
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1YLC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1YLC OCA].
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<StructureSection load='1ylc' size='340' side='right'caption='[[1ylc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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[[Category: Protein complex]]
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== Structural highlights ==
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[[Category: Rattus norvegicus]]
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<table><tr><td colspan='2'>[[1ylc]] 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=1YLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YLC FirstGlance]. <br>
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[[Category: Trypsin]]
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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]] 1.7&#8491;</td></tr>
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[[Category: Brown, C K.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[Category: Ohlendorf, D H.]]
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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=1ylc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ylc OCA], [https://pdbe.org/1ylc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ylc RCSB], [https://www.ebi.ac.uk/pdbsum/1ylc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ylc ProSAT]</span></td></tr>
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[[Category: CA]]
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</table>
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[[Category: SO4]]
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== Function ==
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[[Category: bpti]]
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[https://www.uniprot.org/uniprot/TRY2_RAT TRY2_RAT]
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[[Category: pancreatic trypsin inhibitor]]
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== Evolutionary Conservation ==
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[[Category: trypsin ii]]
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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/yl/1ylc_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=1ylc 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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Crystal structures, at 1.7 A resolution, were solved for complexes between each of two chemically synthesized partially folded analogues of bovine pancreatic trypsin inhibitor (BPTI) with the proteolytically inactive rat trypsin mutant S195A. The BPTI analogue termed [14-38](Abu) retains only the disulfide bond between Cys14 and Cys38, while Cys5, Cys30, Cys51, and Cys55 are replaced by isosteric alpha-amino-n-butyric acid residues. The analogue K26P,A27D[14-38](Abu) contains two further replacements, by statistically favored residues, in the type I beta-turn that has been suggested to be a main site for initiation of BPTI folding. As a control, the structure of the complex between S195A trypsin and wild-type BPTI was also solved. Despite significant differences in the degree of structure detected among these three BPTIs in solution by several biophysical techniques, their tertiary folds once bound to S195A trypsin in a crystalline lattice are essentially superimposable.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:31 2008''
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Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin.,Getun IV, Brown CK, Tulla-Puche J, Ohlendorf D, Woodward C, Barany G J Mol Biol. 2008 Jan 18;375(3):812-23. Epub 2007 Nov 6. PMID:18054043<ref>PMID:18054043</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ylc" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[BPTI 3D structures|BPTI 3D structures]]
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*[[Trypsin 3D structures|Trypsin 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: Rattus norvegicus]]
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[[Category: Brown CK]]
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[[Category: Ohlendorf DH]]

Current revision

Trypsin/BPTI complex mutant

PDB ID 1ylc

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