1kwi: Difference between revisions

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<StructureSection load='1kwi' size='340' side='right'caption='[[1kwi]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
<StructureSection load='1kwi' size='340' side='right'caption='[[1kwi]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1kwi]] 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=1KWI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KWI FirstGlance]. <br>
<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='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>
</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'>[http://proteopedia.org/fgij/fg.htm?mol=1kwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwi OCA], [http://pdbe.org/1kwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kwi RCSB], [http://www.ebi.ac.uk/pdbsum/1kwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwi ProSAT]</span></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>
</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=1kwi 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=1kwi 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 1kwi" 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: Mad]]
[[Category: Protegrin]]
[[Category: Selenocystine]]

Revision as of 11:04, 3 April 2024

Crystal Structure Analysis of the Cathelicidin Motif of ProtegrinsCrystal Structure Analysis of the Cathelicidin Motif of Protegrins

Structural highlights

1kwi is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.19Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PG3_PIG Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1kwi, resolution 2.19Å

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OCA
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