1yuh: Difference between revisions
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[[Image:1yuh.jpg|left|200px]] | [[Image:1yuh.jpg|left|200px]] | ||
'''FAB FRAGMENT''' | {{Structure | ||
|PDB= 1yuh |SIZE=350|CAPTION= <scene name='initialview01'>1yuh</scene>, resolution 3.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NP:4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID'>NP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''FAB FRAGMENT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1YUH is a [ | 1YUH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUH OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8544863 8544863] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Amzel, L M.]] | [[Category: Amzel, L M.]] | ||
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[[Category: lambda light chain]] | [[Category: lambda light chain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:27:39 2008'' | ||
Revision as of 13:27, 20 March 2008
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| 1yuh, resolution 3.0Å | |||||||||||||
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| Ligands: | NP | ||||||||||||
| 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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