1p4t: Difference between revisions

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[[Image:1p4t.~~jpg~~|left|200px]]

[[Image:1p4t.png|left|200px]]

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~~'''~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12716881}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12716881 is the PubMed ID number.

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==About this Structure==

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[[Category: Beta barrel]]

[[Category: Outer membrane protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 04~~:41:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:25:19 2008''

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-[[Image:1p4t.jpg|left|200px]]
+{{Seed}}
+[[Image:1p4t.png|left|200px]]
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 {{STRUCTURE_1p4t|  PDB=1p4t  |  SCENE=  }}
-'''Crystal structure of Neisserial surface protein A (NspA)'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12716881}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12716881 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12716881}}
 ==About this Structure==
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 [[Category: Beta barrel]]
 [[Category: Outer membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:41:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:25:19 2008''