2brr

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[[Image:2brr.gif|left|200px]]<br /><applet load="2brr" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2brr.gif|left|200px]]
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caption="2brr, resolution 1.95&Aring;" />
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'''COMPLEX OF THE NEISSERIAL PORA P1.4 EPITOPE PEPTIDE AND TWO FAB-FRAGMENTS (ANTIBODY MN20B9.34)'''<br />
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{{Structure
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|PDB= 2brr |SIZE=350|CAPTION= <scene name='initialview01'>2brr</scene>, resolution 1.95&Aring;
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|SITE= <scene name='pdbsite=AC1:Acy+Binding+Site+For+Chain+X'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''COMPLEX OF THE NEISSERIAL PORA P1.4 EPITOPE PEPTIDE AND TWO FAB-FRAGMENTS (ANTIBODY MN20B9.34)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BRR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NH2:'>NH2</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Acy+Binding+Site+For+Chain+X'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BRR OCA].
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2BRR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BRR OCA].
==Reference==
==Reference==
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Crystal structure of an Anti-meningococcal subtype P1.4 PorA antibody provides basis for peptide-vaccine design., Oomen CJ, Hoogerhout P, Kuipers B, Vidarsson G, van Alphen L, Gros P, J Mol Biol. 2005 Sep 2;351(5):1070-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16038932 16038932]
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Crystal structure of an Anti-meningococcal subtype P1.4 PorA antibody provides basis for peptide-vaccine design., Oomen CJ, Hoogerhout P, Kuipers B, Vidarsson G, van Alphen L, Gros P, J Mol Biol. 2005 Sep 2;351(5):1070-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16038932 16038932]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:05:51 2008''

Revision as of 14:05, 20 March 2008

Image:2brr.gif


PDB ID 2brr

Drag the structure with the mouse to rotate
, resolution 1.95Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



COMPLEX OF THE NEISSERIAL PORA P1.4 EPITOPE PEPTIDE AND TWO FAB-FRAGMENTS (ANTIBODY MN20B9.34)


Overview

In various western countries, subtype P1.4 of Neisseria meningitidis serogroup B causes the greatest incidence of meningococcal disease. To investigate the molecular recognition of this subtype, we crystallised a peptide (P1HVVVNNKVATH(P11)), corresponding to the subtype P1.4 epitope sequence of outer membrane protein PorA, in complex with a Fab fragment of the bactericidal antibody MN20B9.34 directed against this epitope. Structure determination at 1.95 A resolution revealed a unique complex of one P1.4 antigen peptide bound to two identical Fab fragments. One Fab recognises the putative epitope residues in a 2:2 type I beta-turn at residues P5NNKV(P8), whereas the other Fab binds the C-terminal residues of the peptide that we consider a crystallisation artefact. Interestingly, recognition of the P1.4 epitope peptide is mediated almost exclusively through the complementarity-determining regions of the heavy chain. We exploited the observed turn conformation for designing conformationally restricted cyclic peptides for use as a peptide vaccine. The conformational stability of the two peptide designs was assessed by molecular dynamics simulations. Unlike the linear peptide, both cyclic peptides, conjugated to tetanus toxoid as a carrier protein, elicited antibody responses in mice that recognised meningococci of subtype P1.7-2,4. Serum bactericidal assays showed that some, but not all, of the sera induced with the cyclic peptide conjugates could activate the complement system with titres that were very high compared to the titres induced by complete PorA protein in its native conformation administered in outer membrane vesicles.

About this Structure

2BRR is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of an Anti-meningococcal subtype P1.4 PorA antibody provides basis for peptide-vaccine design., Oomen CJ, Hoogerhout P, Kuipers B, Vidarsson G, van Alphen L, Gros P, J Mol Biol. 2005 Sep 2;351(5):1070-80. PMID:16038932

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