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New page: left|200px<br /> <applet load="1mfe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mfe, resolution 2.0Å" /> '''RECOGNITION OF A CEL...
 
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[[Image:1mfe.gif|left|200px]]<br />
[[Image:1mfe.gif|left|200px]]<br /><applet load="1mfe" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1mfe" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1mfe, resolution 2.0&Aring;" />
caption="1mfe, resolution 2.0&Aring;" />
'''RECOGNITION OF A CELL-SURFACE OLIGO-SACCHARIDE OF PATHOGENIC SALMONELLA BY AN ANTIBODY FAB FRAGMENT'''<br />
'''RECOGNITION OF A CELL-SURFACE OLIGO-SACCHARIDE OF PATHOGENIC SALMONELLA BY AN ANTIBODY FAB FRAGMENT'''<br />


==Overview==
==Overview==
The 2.05 angstrom (A) resolution crystal structure of a, dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition, site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains and a structured, water molecule, rather than the carboxylic acid and amide side chains that, are features of transport and other carbohydrate binding proteins. A, trisaccharide epitope of a branched bacterial lipopolysaccharide fills, this hydrophobic pocket (8 A deep by 7 A wide) in an entropy-assisted, association (association constant = 2.05 x 10(5) liters per mole, enthalpy, = -20.5 +/- 1.7 kilojoules per mole, and temperature times entropy = +10.0, +/- 2.9 kilojoules per mole). The requirement for the complementarity of, van der Waals surfaces and the requirements of saccharide-saccharide and, protein-saccharide hydrogen-bonding networks determine the antigen, conformation adopted in the bound state.
The 2.05 angstrom (A) resolution crystal structure of a dodecasaccharide-Fab complex revealed an unusual carbohydrate recognition site, defined by aromatic amino acids and a structured water molecule, rather than the carboxylic acid and amide side chains and a structured water molecule, rather than the carboxylic acid and amide side chains that are features of transport and other carbohydrate binding proteins. A trisaccharide epitope of a branched bacterial lipopolysaccharide fills this hydrophobic pocket (8 A deep by 7 A wide) in an entropy-assisted association (association constant = 2.05 x 10(5) liters per mole, enthalpy = -20.5 +/- 1.7 kilojoules per mole, and temperature times entropy = +10.0 +/- 2.9 kilojoules per mole). The requirement for the complementarity of van der Waals surfaces and the requirements of saccharide-saccharide and protein-saccharide hydrogen-bonding networks determine the antigen conformation adopted in the bound state.


==About this Structure==
==About this Structure==
1MFE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MFE OCA].  
1MFE is a [http://en.wikipedia.org/wiki/Protein_complex 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=1MFE OCA].  


==Reference==
==Reference==
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]


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