1p4t
From Proteopedia
|
Crystal structure of Neisserial surface protein A (NspA)
Overview
The neisserial surface protein A (NspA) from Neisseria meningitidis is a, promising vaccine candidate because it is highly conserved among, meningococcal strains and induces bactericidal antibodies. NspA is a, homolog of the Opa proteins, which mediate adhesion to host cells. Here, we present the crystal structure of NspA, determined to 2.55-A resolution., NspA forms an eight-stranded antiparallel beta-barrel. The four loops at, the extracellular side of the NspA molecule form a long cleft, which, contains mainly hydrophobic residues and harbors a detergent molecule, suggesting that the protein might function in the binding of hydrophobic, ligands, such as lipids. In addition, the structure provides a starting, point for structure-based vaccine design.
About this Structure
1P4T is a Single protein structure of sequence from Neisseria meningitidis with SO4, CXE and ETA as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential., Vandeputte-Rutten L, Bos MP, Tommassen J, Gros P, J Biol Chem. 2003 Jul 4;278(27):24825-30. Epub 2003 Apr 26. PMID:12716881
Page seeded by OCA on Sun Nov 25 01:58:57 2007
