1lxe: Difference between revisions

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<StructureSection load='1lxe' size='340' side='right'caption='[[1lxe]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1lxe' size='340' side='right'caption='[[1lxe]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1lxe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LXE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1lxe]] 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=1LXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LXE FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kwi|1kwi]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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 PIG])</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=1lxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxe OCA], [https://pdbe.org/1lxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lxe RCSB], [https://www.ebi.ac.uk/pdbsum/1lxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lxe ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1lxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxe OCA], [http://pdbe.org/1lxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lxe RCSB], [http://www.ebi.ac.uk/pdbsum/1lxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lxe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PG3_PIG PG3_PIG]] Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro.  
[https://www.uniprot.org/uniprot/PG3_PIG PG3_PIG] Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1lxe ConSurf].
</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=1lxe ConSurf].
<div style="clear:both"></div>
<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.
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>
</div>
<div class="pdbe-citations 1lxe" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Protegrin|Protegrin]]
*[[Protegrin|Protegrin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pig]]
[[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: Antimicrobial protein]]
[[Category: Cathelicidin motif]]
[[Category: Disulfide]]
[[Category: Domain swapping]]
[[Category: Protegrin]]
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