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1lxe
From Proteopedia
(New page: 200px<br /><applet load="1lxe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxe, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1lxe.gif|left|200px]]<br /><applet load="1lxe" size=" | + | [[Image:1lxe.gif|left|200px]]<br /><applet load="1lxe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lxe, resolution 2.50Å" /> | caption="1lxe, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CATHELICIDIN MOTIF OF PROTEGRINS'''<br /> | '''CRYSTAL STRUCTURE OF THE CATHELICIDIN MOTIF OF PROTEGRINS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cathelicidins are a family of antimicrobial proteins isolated from | + | 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== | ==About this Structure== | ||
| - | 1LXE 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:// | + | 1LXE 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dumas, C.]] | [[Category: Dumas, C.]] | ||
[[Category: Hoh, F.]] | [[Category: Hoh, F.]] | ||
| - | [[Category: Sanchez, J | + | [[Category: Sanchez, J F.]] |
| - | [[Category: Strub, M | + | [[Category: Strub, M P.]] |
[[Category: cathelicidin motif]] | [[Category: cathelicidin motif]] | ||
[[Category: disulfide]] | [[Category: disulfide]] | ||
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[[Category: protegrin]] | [[Category: protegrin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:21 2008'' |
Revision as of 11:49, 21 February 2008
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CRYSTAL STRUCTURE OF THE CATHELICIDIN MOTIF OF PROTEGRINS
Overview
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
1LXE is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:49:21 2008
