5n4j

human Fab fragment 10C3 against NHBA from Neisseria meningitidis

spinqualitylabelsall models 5n4j, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n4j is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.503Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Neisserial heparin-binding antigen (NHBA) is a surface-exposed lipoprotein from Neisseria meningitidis and is a component of the meningococcus B vaccine Bexsero. As part of a study to characterize the three-dimensional structure of NHBA and the molecular basis of the human immune response to Bexsero, the crystal structures of two fragment antigen-binding domains (Fabs) isolated from human monoclonal antibodies targeting NHBA were determined. Through a high-resolution analysis of the organization and the amino-acid composition of the CDRs, these structures provide broad insights into the NHBA epitopes recognized by the human immune system. As expected, these Fabs also show remarkable structural conservation, as shown by a structural comparison of 15 structures of apo Fab 10C3 which were obtained from crystals grown in different crystallization conditions and were solved while searching for a complex with a bound NHBA fragment or epitope peptide. This study also provides indirect evidence for the intrinsically disordered nature of two N-terminal regions of NHBA. Crystal structures of human Fabs targeting the Bexsero meningococcal vaccine antigen NHBA.,Maritan M, Cozzi R, Lo Surdo P, Veggi D, Bottomley MJ, Malito E Acta Crystallogr F Struct Biol Commun. 2017 Jun 1;73(Pt 6):305-314. doi:, 10.1107/S2053230X17006021. Epub 2017 May 11. PMID:28580917 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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