7jtr

Complex of maltose-binding protein (MBP) with single-chain Fv (scFv)

spinqualitylabelsall models 7jtr, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7jtr is a 8 chain structure with sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: CL, GLC, PRD_900001 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMed Maltose binding protein (MBP) is used in recombinant protein expression as an affinity and solubility tag. The monoclonal antibody B48 binds MBP tightly and has no cross-reactivity to other proteins in an Escherichia coli lysate. This high level of specificity suggested that MBP contains an epitope that could prove useful as a purification and visualization tag for proteins expressed in E. coli. To discover the MBP epitope, a co-crystal structure was determined for MBP bound to its antibody and four amino acids of MBP were identified as critical for the binding interaction. Fusions of various fragments of MBP to the glutathione S-transferase protein were engineered in order to identify the smallest fragment still recognized by the alpha-MBP antibody. Stabilization of the epitope via mutational engineering resulted in a minimized 14 amino-acid tag. A useful epitope tag derived from maltose binding protein.,Lenon M, Ke N, Ren G, Meuser ME, Loll PJ, Riggs P, Berkmen M Protein Sci. 2021 Jun;30(6):1235-1246. doi: 10.1002/pro.4088. PMID:33896065 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Maltose-binding protein 3D structures Monoclonal Antibodies 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA