2ihl
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(New page: 200px<br /> <applet load="2ihl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ihl, resolution 1.4Å" /> '''LYSOZYME (E.C.3.2.1....)
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Revision as of 07:44, 18 November 2007
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LYSOZYME (E.C.3.2.1.17) (JAPANESE QUAIL)
Overview
Although antibodies are highly specific, cross-reactions are frequently, observed. To understand the molecular basis of this phenomenon, we studied, the anti-hen egg lysozyme (HEL) monoclonal antibody (mAb) D11.15, which, cross-reacts with several avian lysozymes, in some cases with a higher, affinity (heteroclitic binding) than for HEL. We have determined the, crystal structure of the Fv fragment of D11.15 complexed with pheasant egg, lysozyme (PHL). In addition, we have determined the structure of PHL, Guinea fowl egg lysozyme, and Japanese quail egg lysozyme. Differences in, the affinity of D11.15 for the lysozymes appear to result from sequence, substitutions in these antigens at the interface with the antibody. More, generally, cross-reactivity is seen to require a stereochemically, permissive environment for the variant antigen residues at the, antibody-antigen interface.
About this Structure
2IHL is a Single protein structure of sequence from Coturnix japonica with NA as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex., Chitarra V, Alzari PM, Bentley GA, Bhat TN, Eisele JL, Houdusse A, Lescar J, Souchon H, Poljak RJ, Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7711-5. PMID:8356074
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