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1cgh

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(New page: 200px<br /> <applet load="1cgh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cgh, resolution 1.8&Aring;" /> '''HUMAN CATHEPSIN G'''...)
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[[Image:1cgh.gif|left|200px]]<br />
 
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<applet load="1cgh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cgh, resolution 1.8&Aring;" />
 
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'''HUMAN CATHEPSIN G'''<br />
 
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==Overview==
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==Human cathepsin G==
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The crystal structure of human neutrophil cathepsin G, complexed with the, peptidyl phosphonate inhibitor Suc-Val-Pro-PheP-(OPh)2, has been, determined to a resolution of 1.8 A using Patterson search techniques. The, cathepsin G structure shows the polypeptide fold characteristic of, trypsin-like serine proteinases and is especially similar to rat mast cell, proteinase II. Unique to cathepsin G, however, is the presence of Glu226, (chymotrypsinogen numbering), which is situated at the bottom of the S1, specificity pocket, dividing it into two compartments. For this reason, the benzyl side chain of the inhibitor PheP residue does not fully occupy, the pocket but is, instead, located at its entrance. Its positively, charged equatorial edge is involved in a favourable electrostatic, interaction with the negatively charged carboxylate group of Glu226., Arrangement of this Glu226 carboxylate would also allow accommodation of a, Lys side chain in this S1 pocket, in agreement with the recently observed, cathepsin G preference for Lys and Phe at P1. The cathepsin G complex with, the covalently bound phosphonate inhibitor mimics a tetrahedral substrate, intermediate. A comparison of the Arg surface distributions of cathepsin, G, leukocyte elastase and rat mast cell protease II shows no simple common, recognition pattern for a mannose-6-phosphate receptor-independent, targeting mechanism for sorting of these granular proteinases.
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<StructureSection load='1cgh' size='340' side='right'caption='[[1cgh]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cgh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CGH 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]] 1.8&#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=1ZG:N-(3-CARBOXYPROPANOYL)-L-VALYL-N-{(1R)-1-[(S)-HYDROXY(OXIDO)PHOSPHANYL]-2-PHENYLETHYL}-L-PROLINAMIDE'>1ZG</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=1cgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cgh OCA], [https://pdbe.org/1cgh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cgh RCSB], [https://www.ebi.ac.uk/pdbsum/1cgh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cgh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CATG_HUMAN CATG_HUMAN] Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe-CH2Cl and phenylmethylsulfonyl fluoride.<ref>PMID:8194606</ref> <ref>PMID:1861080</ref> <ref>PMID:1937776</ref>
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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/cg/1cgh_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=1cgh 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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1CGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Cathepsin_G Cathepsin G], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.20 3.4.21.20] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CGH OCA].
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*[[Cathepsin 3D structures|Cathepsin 3D structures]]
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== References ==
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==Reference==
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<references/>
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The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities., Hof P, Mayr I, Huber R, Korzus E, Potempa J, Travis J, Powers JC, Bode W, EMBO J. 1996 Oct 15;15(20):5481-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8896442 8896442]
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__TOC__
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[[Category: Cathepsin G]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bode, W.]]
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[[Category: Bode W]]
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[[Category: Hof, P.]]
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[[Category: Hof P]]
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[[Category: complex (serine protease/inhibitor)]]
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[[Category: inflammation]]
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[[Category: inhibitor]]
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[[Category: serine protease]]
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[[Category: specificity]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:21:39 2007''
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Current revision

Human cathepsin G

PDB ID 1cgh

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