1p4t: Difference between revisions
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'''Crystal structure of Neisserial surface protein A (NspA)''' | '''Crystal structure of Neisserial surface protein A (NspA)''' | ||
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[[Category: Tommassen, J.]] | [[Category: Tommassen, J.]] | ||
[[Category: Vandeputte-Rutten, L.]] | [[Category: Vandeputte-Rutten, L.]] | ||
[[Category: | [[Category: Beta barrel]] | ||
[[Category: | [[Category: Outer membrane protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:41:15 2008'' | |||
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Revision as of 01:41, 3 May 2008
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. 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 Sat May 3 04:41:15 2008