1c08
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(New page: 200px<br /> <applet load="1c08" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c08, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 07:20, 18 November 2007
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CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN LYSOZYME COMPLEX
Overview
In order to address the recognition mechanism of the fragments of antibody, variable regions, termed Fv, toward their target antigen, an x-ray crystal, structure of an anti-hen egg white lysozyme antibody (HyHEL-10) Fv, fragment complexed with its cognate antigen, hen egg white lysozyme (HEL), was solved at 2.3 A. The overall structure of the complex is similar to, that reported in a previous article dealing with the Fab fragment-HEL, complex (PDB ID code,). However, the areas of Fv covered by HEL upon, complex formation increased by about 100 A(2) in comparison with the, Fab-HEL complex, and two local structural differences were observed in the, heavy chain of the variable region (VH). In addition, small but, significant local structural changes were observed in the antigen, HEL., The x-ray data permitted the identification of two water molecules between, the VH and HEL and six water molecules retained in the interface between, the antigen and the light chain complementarity determining regions (CDRs), 2 and 3 (CDR-L2 and CDR-L3). These water molecules bridge the, antigen-antibody interface through hydrogen bond formation in the VL-HEL, interface. Eleven water molecules were found to complete the imperfect, VH-VL interface, suggesting that solvent molecules mediate the, stabilization of interaction between variable regions. These results, suggest that the unfavorable effect of deletion of constant regions on the, antigen-antibody interaction is compensated by an increase in favorable, interactions, including structural changes in the antigen-antibody, interface and solvent-mediated hydrogen bond formation upon complex, formation, which may lead to a minimum decreased affinity of the antibody, Fv fragment toward its antigen.
About this Structure
1C08 is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of anti-Hen egg white lysozyme antibody (HyHEL-10) Fv-antigen complex. Local structural changes in the protein antigen and water-mediated interactions of Fv-antigen and light chain-heavy chain interfaces., Kondo H, Shiroishi M, Matsushima M, Tsumoto K, Kumagai I, J Biol Chem. 1999 Sep 24;274(39):27623-31. PMID:10488102
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