1dkj

OverviewOverview

The HyHEL-5 antibody has more than a thousandfold lower affinity for, bobwhite quail lysozyme (BWQL) than for hen egg-white lysozyme (HEL). Four, sequence differences exist between BWQL and HEL, of which only one is, involved in the interface with the Fab. The structure of bobwhite quail, lysozyme has been determined in the uncomplexed state in two different, crystal forms and in the complexed state with HyHEL-5, an antihen, egg-white lysozyme Fab. Similar backbone conformations are observed in the, three molecules of the two crystal forms of uncomplexed BWQL, although, they show considerable variability in side-chain conformation. A, relatively mobile segment in uncomplexed BWQL is observed to be part of, the HyHEL-5 epitope. No major backbone conformational differences are, observed in the lysozyme upon complex formation, but side-chain, conformational differences are seen in surface residues that are involved, in the interface with the antibody. The hydrogen bonding in the interface, between BWQL and HyHEL-5 is similar to that in previously determined, lysozyme-HyHEL-5 complexes.

About this StructureAbout this Structure

1DKJ is a Single protein structure of sequence from Colinus virginianus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment., Chacko S, Silverton EW, Smith-Gill SJ, Davies DR, Shick KA, Xavier KA, Willson RC, Jeffrey PD, Chang CY, Sieker LC, Sheriff S, Proteins. 1996 Sep;26(1):55-65. PMID:8880929

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