1a7l

DOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS IN THE FORM OF AN INSERTED PEPTIDE SEGMENT IN MALTODEXTRIN-BINDING PROTEINDOMINANT B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS IN THE FORM OF AN INSERTED PEPTIDE SEGMENT IN MALTODEXTRIN-BINDING PROTEIN

Structural highlights 1a7l is a 3 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: , 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We report here the crystal structure of MalE-B363, a recombinant construction of maltodextrin-binding protein bearing a dominant B-cell epitope sequence from the preS2 region of the hepatitis B surface antigen. The inserted peptide sequence, which replaces the seven carboxy-terminal residues of maltodextrin-binding protein, carries the 14 amino acid residue epitope contained between residues 132 and 145 from the preS2 region. The epitope sequence is flanked on either side by additional residues that result from the genetically engineered insertion, bringing the total length of the foreign peptide to 26 amino acid residues. The hybrid protein has been previously shown to be recognised by monoclonal antibodies elicited by the native viral antigen. Three independent molecules of MalE-B363 are present in the asymmetric unit of the crystal. All 14 epitope residues could be traced for one molecule, ten epitope residues had significant electron density for the second, but no density was visible for the epitope of the third. The conformation of the amino-terminal segment of the epitope from Gln132(e) to Gly138(e) is similar in the two molecules of MalE-B363 for which the foreign peptide could be traced. Moreover, the conformation of a smaller segment, comprising residues Asp133(e) to Arg137(e), is similar to that present in the previously determined crystal structure of MalE-B133, another insertion/deletion mutant of maltodextrin-binding protein bearing the preS2 epitope. The presence of a common structural motif for the same sequence in disparate molecular environments suggests that this conformation might be present also in the native viral antigen. This could provide a structural basis to explain the cross-reactivity of anti-preS2 monoclonal antibodies with these hybrid proteins. Crystal structure of a dominant B-cell epitope from the preS2 region of hepatitis B virus in the form of an inserted peptide segment in maltodextrin-binding protein.,Saul FA, Vulliez-le Normand B, Lema F, Bentley GA J Mol Biol. 1998 Jul 10;280(2):185-92. PMID:9654443 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1a7l, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image