1fh5
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CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MONOCLONAL ANTIBODY MAK33
OverviewOverview
The Fab fragment of the murine monoclonal antibody, MAK33, directed, against human creatine kinase of the muscle-type, was crystallized and the, three-dimensional structure was determined to 2.9 A. The antigen-binding, surface of MAK33 shows a convex overall shape typical for immunoglobulins, binding large antigens. The structure allows us to analyze the environment, of cis-prolyl-peptide bonds whose isomerization is of key importance in, the folding process. These residues seem to be involved with not only, domain stability but also seem to play a role in the association of heavy, and light chains, reinforcing the importance of beta-strand recognition in, antibody assembly. The structure also allows the localization of segments, of primary sequence postulated to represent binding sites for the, ER-specific chaperone BiP within the context of the entire Fab fragment., These sequences are found primarily in beta-strands that are necessary for, interactions between the individual domains.
About this StructureAbout this Structure
1FH5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bip., Augustine JG, de La Calle A, Knarr G, Buchner J, Frederick CA, J Biol Chem. 2001 Feb 2;276(5):3287-94. Epub 2000 Oct 17. PMID:11036070
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