1yuh
From Proteopedia
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|PDB= 1yuh |SIZE=350|CAPTION= <scene name='initialview01'>1yuh</scene>, resolution 3.0Å | |PDB= 1yuh |SIZE=350|CAPTION= <scene name='initialview01'>1yuh</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NP:4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID'>NP</scene> | + | |LIGAND= <scene name='pdbligand=NP:4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC+ACID'>NP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yuh OCA], [http://www.ebi.ac.uk/pdbsum/1yuh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yuh RCSB]</span> | ||
}} | }} | ||
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[[Category: Strand, M.]] | [[Category: Strand, M.]] | ||
[[Category: Yuhasz, S C.]] | [[Category: Yuhasz, S C.]] | ||
| - | [[Category: NP]] | ||
[[Category: anti-nitrophenol]] | [[Category: anti-nitrophenol]] | ||
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
[[Category: lambda light chain]] | [[Category: lambda light chain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:22:55 2008'' |
Revision as of 22:22, 30 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FAB FRAGMENT
Overview
Affinity maturation of the immune response to nitrophenol-containing antigens has been extensively investigated. Significant strides made during the past several years with the advent of PCR technology have provided a wealth of biochemical knowledge. Structural investigations of the phenomena have however been limited. We have determined the three-dimensional structure of the Fab fragment of 88C6/12, an anti-4-hydroxy-3-nitrophenyl acetic acid antibody complexed with the immunizing hapten and with a heteroclitic iodinated hapten. The crystallographic structure of the complexes reveals that the binding is stabilized by a number of hydrogen bonds and extensive van der Waals interactions between the hapten and the antibody. In addition, the Fab binding pocket contains a region of positive electrostatic potential well suited for interaction with the predominant resonance form of the nitrophenyl ring system. The observed heteroclicity towards the iodinated hapten is not a direct result of iodine-protein interactions, but results from the enhanced stability in the iodinated ring of the resonance form that binds the antibody. In addition this investigation provides a rationale for the strong preference for the substitution in the heavy chain from the germ-line gene encoded Trp 33 to Leu 33 in the mature anti-nitrophenol response.
About this Structure
1YUH is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structural analysis of affinity maturation: the three-dimensional structures of complexes of an anti-nitrophenol antibody., Yuhasz SC, Parry C, Strand M, Amzel LM, Mol Immunol. 1995 Oct;32(14-15):1143-55. PMID:8544863
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