1kwi

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(New page: 200px<br /><applet load="1kwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kwi, resolution 2.19&Aring;" /> '''Crystal Structure An...)
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[[Image:1kwi.jpg|left|200px]]<br /><applet load="1kwi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kwi, resolution 2.19&Aring;" />
 
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'''Crystal Structure Analysis of the Cathelicidin Motif of Protegrins'''<br />
 
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==Overview==
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==Crystal Structure Analysis of the Cathelicidin Motif of Protegrins==
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Cathelicidins are a family of antimicrobial proteins isolated from, leucocytes and epithelia cells that contribute to the innate host defense, mechanisms in mammalians. Located in the C-terminal part of the, holoprotein, the cathelicidin-derived antimicrobial peptide is liberated, by a specific protease cleavage. Here, we report the X-ray structure of, the cathelicidin motif of protegrin-3 solved by MAD phasing using the, selenocysteine-labeled protein. Its overall structure represents a fold, homologous to the cystatin family and adopts two native states, a monomer, and a domain-swapped dimer. This crystal structure is the first example of, a structural characterization of the highly conserved cathelicidin motif, and thus provides insights into the possible mechanism of activation of, the antimicrobial protegrin peptide.
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<StructureSection load='1kwi' size='340' side='right'caption='[[1kwi]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kwi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KWI 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]] 2.19&#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=1kwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwi OCA], [https://pdbe.org/1kwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kwi RCSB], [https://www.ebi.ac.uk/pdbsum/1kwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PG3_PIG PG3_PIG] Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro.
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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/kw/1kwi_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=1kwi 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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Cathelicidins are a family of antimicrobial proteins isolated from leucocytes and epithelia cells that contribute to the innate host defense mechanisms in mammalians. Located in the C-terminal part of the holoprotein, the cathelicidin-derived antimicrobial peptide is liberated by a specific protease cleavage. Here, we report the X-ray structure of the cathelicidin motif of protegrin-3 solved by MAD phasing using the selenocysteine-labeled protein. Its overall structure represents a fold homologous to the cystatin family and adopts two native states, a monomer, and a domain-swapped dimer. This crystal structure is the first example of a structural characterization of the highly conserved cathelicidin motif and thus provides insights into the possible mechanism of activation of the antimicrobial protegrin peptide.
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==About this Structure==
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Structure of the cathelicidin motif of protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein.,Sanchez JF, Hoh F, Strub MP, Aumelas A, Dumas C Structure. 2002 Oct;10(10):1363-70. PMID:12377122<ref>PMID:12377122</ref>
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1KWI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KWI 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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Structure of the cathelicidin motif of protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein., Sanchez JF, Hoh F, Strub MP, Aumelas A, Dumas C, Structure. 2002 Oct;10(10):1363-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12377122 12377122]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1kwi" style="background-color:#fffaf0;"></div>
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[[Category: Sus scrofa]]
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[[Category: Aumelas, A.]]
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[[Category: Dumas, C.]]
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[[Category: Hoh, F.]]
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[[Category: Sanchez, J.F.]]
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[[Category: Strub, M.P.]]
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[[Category: cathelicidin motif]]
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[[Category: disulfide]]
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[[Category: mad]]
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[[Category: protegrin]]
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[[Category: selenocystine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:01:23 2007''
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==See Also==
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*[[Protegrin|Protegrin]]
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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: Large Structures]]
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[[Category: Sus scrofa]]
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[[Category: Aumelas A]]
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[[Category: Dumas C]]
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[[Category: Hoh F]]
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[[Category: Sanchez JF]]
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[[Category: Strub MP]]

Current revision

Crystal Structure Analysis of the Cathelicidin Motif of Protegrins

PDB ID 1kwi

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