1bnb
From Proteopedia
(New page: 200px<br /><applet load="1bnb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bnb" /> '''SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA...) |
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| - | [[Image:1bnb.gif|left|200px]]<br /><applet load="1bnb" size=" | + | [[Image:1bnb.gif|left|200px]]<br /><applet load="1bnb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bnb" /> | caption="1bnb" /> | ||
'''SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN 12: THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT OF THE CLASSICAL DEFENSINS'''<br /> | '''SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN 12: THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT OF THE CLASSICAL DEFENSINS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure is reported for bovine neutrophil beta-defensin-12 | + | The solution structure is reported for bovine neutrophil beta-defensin-12 (BNBD-12), a member of the beta-defensin family of antimicrobial peptides. Structural constraints in the form of proton-proton distances, dihedral angles, and hydrogen bond constraints were derived from two-dimensional, homonuclear magnetic resonance spectroscopy experiments. The three-dimensional structure of BNBD-12 was calculated using distance geometry and restrained molecular dynamics. An ensemble of structures with low NOE constraint violation energies revealed a precisely defined triple-stranded, antiparallel beta-sheet as the structural core of the peptide. The N-terminal beta-strand and three locally well-defined tight turns form a hydrophobic face. Conserved isoleucine and glycine residues form a beta-bulge structure which initiates a beta-hairpin secondary structure motif composed of the second and C-terminal beta-strands. The beta-hairpin contains numerous charged residues and forms the cationic face of BNBD-12. The N-terminal residues were found to be disordered, due to an absence of tertiary NOEs. The triple-stranded beta-sheet, the beta-bulge preceding the hairpin, and the cationic/hydrophobic amphiphilic character are definitive features of all defensin structures determined to date. Further, we predict that the tracheal antimicrobial peptide (TAP) and the recently described gallinacins will have tertiary structures similar to that of BNBD-12. |
==About this Structure== | ==About this Structure== | ||
| - | 1BNB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1BNB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BNB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Legault, P.]] | [[Category: Legault, P.]] | ||
[[Category: Pardi, A.]] | [[Category: Pardi, A.]] | ||
| - | [[Category: Selsted, M | + | [[Category: Selsted, M E.]] |
| - | [[Category: Zimmermann, G | + | [[Category: Zimmermann, G R.]] |
[[Category: beta-defensin 12]] | [[Category: beta-defensin 12]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:09 2008'' |
Revision as of 09:57, 21 February 2008
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SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN 12: THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT OF THE CLASSICAL DEFENSINS
Overview
The solution structure is reported for bovine neutrophil beta-defensin-12 (BNBD-12), a member of the beta-defensin family of antimicrobial peptides. Structural constraints in the form of proton-proton distances, dihedral angles, and hydrogen bond constraints were derived from two-dimensional, homonuclear magnetic resonance spectroscopy experiments. The three-dimensional structure of BNBD-12 was calculated using distance geometry and restrained molecular dynamics. An ensemble of structures with low NOE constraint violation energies revealed a precisely defined triple-stranded, antiparallel beta-sheet as the structural core of the peptide. The N-terminal beta-strand and three locally well-defined tight turns form a hydrophobic face. Conserved isoleucine and glycine residues form a beta-bulge structure which initiates a beta-hairpin secondary structure motif composed of the second and C-terminal beta-strands. The beta-hairpin contains numerous charged residues and forms the cationic face of BNBD-12. The N-terminal residues were found to be disordered, due to an absence of tertiary NOEs. The triple-stranded beta-sheet, the beta-bulge preceding the hairpin, and the cationic/hydrophobic amphiphilic character are definitive features of all defensin structures determined to date. Further, we predict that the tracheal antimicrobial peptide (TAP) and the recently described gallinacins will have tertiary structures similar to that of BNBD-12.
About this Structure
1BNB is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Solution structure of bovine neutrophil beta-defensin-12: the peptide fold of the beta-defensins is identical to that of the classical defensins., Zimmermann GR, Legault P, Selsted ME, Pardi A, Biochemistry. 1995 Oct 17;34(41):13663-71. PMID:7577957
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