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| - | [[Image:1c08.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1c08.png|left|200px]] |
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| | {{STRUCTURE_1c08| PDB=1c08 | SCENE= }} | | {{STRUCTURE_1c08| PDB=1c08 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN LYSOZYME COMPLEX'''
| + | ===CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN LYSOZYME COMPLEX=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10488102}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10488102 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10488102}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tsumoto, K.]] | | [[Category: Tsumoto, K.]] |
| | [[Category: Antigen-antibody complex]] | | [[Category: Antigen-antibody complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:10:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:01:48 2008'' |
Revision as of 17:01, 30 June 2008
Template:STRUCTURE 1c08
CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN LYSOZYME COMPLEX
Template:ABSTRACT PUBMED 10488102
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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