2op4

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[[Image:2op4.gif|left|200px]]
[[Image:2op4.gif|left|200px]]
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{{Structure
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|PDB= 2op4 |SIZE=350|CAPTION= <scene name='initialview01'>2op4</scene>, resolution 2.85&Aring;
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The line below this paragraph, containing "STRUCTURE_2op4", creates the "Structure Box" on the page.
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|SITE=
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{{STRUCTURE_2op4| PDB=2op4 | SCENE= }}
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|RELATEDENTRY=[[2ntf|2NTF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2op4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2op4 OCA], [http://www.ebi.ac.uk/pdbsum/2op4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2op4 RCSB]</span>
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'''Crystal Structure of Quorum-Quenching Antibody 1G9'''
'''Crystal Structure of Quorum-Quenching Antibody 1G9'''
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==About this Structure==
==About this Structure==
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2OP4 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=2OP4 OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OP4 OCA].
==Reference==
==Reference==
Crystal structures of a quorum-quenching antibody., Debler EW, Kaufmann GF, Kirchdoerfer RN, Mee JM, Janda KD, Wilson IA, J Mol Biol. 2007 May 18;368(5):1392-402. Epub 2007 Mar 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17400249 17400249]
Crystal structures of a quorum-quenching antibody., Debler EW, Kaufmann GF, Kirchdoerfer RN, Mee JM, Janda KD, Wilson IA, J Mol Biol. 2007 May 18;368(5):1392-402. Epub 2007 Mar 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17400249 17400249]
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[[Category: Mus musculus]]
 
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[[Category: Protein complex]]
 
[[Category: Debler, E W.]]
[[Category: Debler, E W.]]
[[Category: Kirchdoerfer, R N.]]
[[Category: Kirchdoerfer, R N.]]
[[Category: Wilson, I A.]]
[[Category: Wilson, I A.]]
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[[Category: antibody]]
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[[Category: Antibody]]
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[[Category: fab]]
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[[Category: Fab]]
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[[Category: homoserine lactone]]
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[[Category: Homoserine lactone]]
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[[Category: immunoglobulin]]
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[[Category: Immunoglobulin]]
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[[Category: induced fit]]
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[[Category: Induced fit]]
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[[Category: quorum sensing]]
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[[Category: Quorum sensing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:21:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:21:05 2008''
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Revision as of 08:21, 4 May 2008

Template:STRUCTURE 2op4

Crystal Structure of Quorum-Quenching Antibody 1G9


Overview

A large number of Gram-negative bacteria employ N-acyl homoserine lactones (AHLs) as signaling molecules in quorum sensing, which is a population density-dependent mechanism to coordinate gene expression. Antibody RS2-1G9 was elicited against a lactam mimetic of the N-acyl homoserine lactone and represents the only reported monoclonal antibody that recognizes the naturally-occuring N-acyl homoserine lactone with high affinity. Due to its high cross-reactivity, RS2-1G9 showed remarkable inhibition of quorum sensing signaling in Pseudomonas aeruginosa, a common opportunistic pathogen in humans. The crystal structure of Fab RS2-1G9 in complex with a lactam analog revealed complete encapsulation of the polar lactam moiety in the antibody-combining site. This mode of recognition provides an elegant immunological solution for tight binding to an aliphatic, lipid-like ligand with a small head group lacking typical haptenic features, such as aromaticity or charge, which are often incorporated into hapten design to generate high-affinity antibodies. The ability of RS2-1G9 to discriminate between closely related AHLs is conferred by six hydrogen bonds to the ligand. Conversely, cross-reactivity of RS2-1G9 towards the lactone is likely to originate from conservation of these hydrogen bonds as well as an additional hydrogen bond to the oxygen of the lactone ring. A short, narrow tunnel exiting at the protein surface harbors a portion of the acyl chain and would not allow entry of the head group. The crystal structure of the antibody without its cognate lactam or lactone ligands revealed a considerably altered antibody-combining site with a closed binding pocket. Curiously, a completely buried ethylene glycol molecule mimics the lactam ring and, thus, serves as a surrogate ligand. The detailed structural delineation of this quorum-quenching antibody will aid further development of an antibody-based therapy against bacterial pathogens by interference with quorum sensing.

About this Structure

Full crystallographic information is available from OCA.

Reference

Crystal structures of a quorum-quenching antibody., Debler EW, Kaufmann GF, Kirchdoerfer RN, Mee JM, Janda KD, Wilson IA, J Mol Biol. 2007 May 18;368(5):1392-402. Epub 2007 Mar 6. PMID:17400249 Page seeded by OCA on Sun May 4 11:21:55 2008

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