1kwi

<StructureSection load='1kwi' size='340' side='right' caption='[[1kwi]], [[Resolution|resolution]] 2.19&Aring;' scene=''>

<table><tr><td colspan='2'>[[1kwi]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KWI FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pg3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kwi RCSB], [http://www.ebi.ac.uk/pdbsum/1kwi PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/PG3_PIG PG3_PIG]] Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kw/1kwi_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Aumelas, A]]

[[Category: Dumas, C]]

[[Category: Hoh, F]]

[[Category: Sanchez, J F]]

[[Category: Strub, M P]]

[[Category: Selenocystine]]