1kwi

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(New page: 200px<br /><applet load="1kwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kwi, resolution 2.19&Aring;" /> '''Crystal Structure An...)
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[[Image:1kwi.jpg|left|200px]]<br /><applet load="1kwi" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kwi, resolution 2.19&Aring;" />
caption="1kwi, resolution 2.19&Aring;" />
'''Crystal Structure Analysis of the Cathelicidin Motif of Protegrins'''<br />
'''Crystal Structure Analysis of the Cathelicidin Motif of Protegrins'''<br />
==Overview==
==Overview==
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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.
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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==
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1KWI 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KWI OCA].
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1KWI 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=1KWI OCA].
==Reference==
==Reference==
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[[Category: Dumas, C.]]
[[Category: Dumas, C.]]
[[Category: Hoh, F.]]
[[Category: Hoh, F.]]
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[[Category: Sanchez, J.F.]]
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[[Category: Sanchez, J F.]]
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[[Category: Strub, M.P.]]
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[[Category: Strub, M P.]]
[[Category: cathelicidin motif]]
[[Category: cathelicidin motif]]
[[Category: disulfide]]
[[Category: disulfide]]
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[[Category: selenocystine]]
[[Category: selenocystine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:01:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:42 2008''

Revision as of 11:38, 21 February 2008

Image:1kwi.jpg

1kwi, resolution 2.19Å

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Crystal Structure Analysis 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

1KWI 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

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