1acb

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(New page: 200px<br /><applet load="1acb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1acb, resolution 2.0&Aring;" /> '''CRYSTAL AND MOLECULAR...)
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[[Image:1acb.gif|left|200px]]<br /><applet load="1acb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1acb, resolution 2.0&Aring;" />
 
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'''CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION==
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The crystal structure of the complex between bovine alpha-chymotrypsin and, the leech (Hirudo medicinalis) protein proteinase inhibitor eglin c has, been refined at 2.0 A resolution to a crystallographic R-factor of 0.167., The structure of the complex includes 2290 protein and 143 solvent atoms., Eglin c is bound to the cognate enzyme through interactions involving 11, residues of the inhibitor (sites P5-P4' in the reactive site loop, P10', and P23') and 17 residues from chymotrypsin. Binding of eglin c to the, enzyme causes a contained hinge-bending movement around residues P4 and, P4' of the inhibitor. The tertiary structure of chymotrypsin is little, affected, with the exception of the 10-13 region, where an ordered, structure for the polypeptide chain is observed. The overall binding mode, is consistent with those found in other serine, proteinase-protein-inhibitor complexes, including those from different, inhibition families. Contained, but significant differences are observed, in the establishment of intramolecular hydrogen bonds and polar, interactions stabilizing the structure of the intact inhibitor, if the, structure of eglin c in its complex with chymotrypsin is compared with, that of other eglin c-serine proteinase complexes.
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<StructureSection load='1acb' size='340' side='right'caption='[[1acb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1acb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ACB 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&#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=1acb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1acb OCA], [https://pdbe.org/1acb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1acb RCSB], [https://www.ebi.ac.uk/pdbsum/1acb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1acb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME] Inhibits both elastase and cathepsin G.
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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/ac/1acb_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=1acb 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 crystal structure of the complex between bovine alpha-chymotrypsin and the leech (Hirudo medicinalis) protein proteinase inhibitor eglin c has been refined at 2.0 A resolution to a crystallographic R-factor of 0.167. The structure of the complex includes 2290 protein and 143 solvent atoms. Eglin c is bound to the cognate enzyme through interactions involving 11 residues of the inhibitor (sites P5-P4' in the reactive site loop, P10' and P23') and 17 residues from chymotrypsin. Binding of eglin c to the enzyme causes a contained hinge-bending movement around residues P4 and P4' of the inhibitor. The tertiary structure of chymotrypsin is little affected, with the exception of the 10-13 region, where an ordered structure for the polypeptide chain is observed. The overall binding mode is consistent with those found in other serine proteinase-protein-inhibitor complexes, including those from different inhibition families. Contained, but significant differences are observed in the establishment of intramolecular hydrogen bonds and polar interactions stabilizing the structure of the intact inhibitor, if the structure of eglin c in its complex with chymotrypsin is compared with that of other eglin c-serine proteinase complexes.
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==About this Structure==
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Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution.,Frigerio F, Coda A, Pugliese L, Lionetti C, Menegatti E, Amiconi G, Schnebli HP, Ascenzi P, Bolognesi M J Mol Biol. 1992 May 5;225(1):107-23. PMID:1583684<ref>PMID:1583684</ref>
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1ACB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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=1ACB 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 and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution., Frigerio F, Coda A, Pugliese L, Lionetti C, Menegatti E, Amiconi G, Schnebli HP, Ascenzi P, Bolognesi M, J Mol Biol. 1992 May 5;225(1):107-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1583684 1583684]
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</div>
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[[Category: Chymotrypsin]]
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<div class="pdbe-citations 1acb" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Amiconi, G.]]
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[[Category: Ascenzi, P.]]
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[[Category: Bolognesi, M.]]
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[[Category: Coda, A.]]
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[[Category: Frigerio, F.]]
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[[Category: Lionetti, C.]]
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[[Category: Menegatti, E.]]
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[[Category: Pugliese, L.]]
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[[Category: Schnebli, H.P.]]
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[[Category: hydrolase(serine protease)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:45:10 2007''
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==See Also==
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*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
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*[[Eglin|Eglin]]
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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: Hirudo medicinalis]]
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[[Category: Large Structures]]
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[[Category: Amiconi G]]
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[[Category: Ascenzi P]]
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[[Category: Bolognesi M]]
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[[Category: Coda A]]
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[[Category: Frigerio F]]
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[[Category: Lionetti C]]
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[[Category: Menegatti E]]
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[[Category: Pugliese L]]
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[[Category: Schnebli HP]]

Current revision

CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION

PDB ID 1acb

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