1kwi: Difference between revisions

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-[[Image:1kwi.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1kwi", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1kwi|  PDB=1kwi  |  SCENE=  }}
-'''Crystal Structure Analysis of the Cathelicidin Motif of Protegrins'''
+==Crystal Structure Analysis of the Cathelicidin Motif of Protegrins==
+<StructureSection load='1kwi' size='340' side='right'caption='[[1kwi]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PG3_PIG PG3_PIG] Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kw/1kwi_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-KWI is a [[Single protein]] structure of sequence from [http://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].
+</div>
+<div class="pdbe-citations 1kwi" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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://www.ncbi.nlm.nih.gov/pubmed/12377122 12377122]
+*[[Protegrin|Protegrin]]
-[[Category: Single protein]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Sus scrofa]]
-[[Category: Aumelas, A.]]
+[[Category: Aumelas A]]
-[[Category: Dumas, C.]]
+[[Category: Dumas C]]
-[[Category: Hoh, F.]]
+[[Category: Hoh F]]
-[[Category: Sanchez, J F.]]
+[[Category: Sanchez JF]]
-[[Category: Strub, M P.]]
+[[Category: Strub MP]]
-[[Category: Cathelicidin motif]]
-[[Category: Disulfide]]
-[[Category: Mad]]
-[[Category: Protegrin]]
-[[Category: Selenocystine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:15:27 2008''