1p4t: Difference between revisions

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[[Image:1p4t.jpg|left|200px]]
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{{STRUCTURE_1p4t|  PDB=1p4t  |  SCENE=  }}  
{{STRUCTURE_1p4t|  PDB=1p4t  |  SCENE=  }}  


'''Crystal structure of Neisserial surface protein A (NspA)'''
===Crystal structure of Neisserial surface protein A (NspA)===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12716881}}


==About this Structure==
==About this Structure==
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[[Category: Beta barrel]]
[[Category: Beta barrel]]
[[Category: Outer membrane protein]]
[[Category: Outer membrane protein]]
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Revision as of 00:25, 29 July 2008

File:1p4t.png

Template:STRUCTURE 1p4t

Crystal structure of Neisserial surface protein A (NspA)

Template:ABSTRACT PUBMED 12716881

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

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