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'''NMR structure of Mini-B, an N-terminal- C-terminal construct from human Surfactant Protein-B (SP-B), in Hexafluoroisopropanol (HFIP)''' | '''NMR structure of Mini-B, an N-terminal- C-terminal construct from human Surfactant Protein-B (SP-B), in Hexafluoroisopropanol (HFIP)''' | ||
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==About this Structure== | ==About this Structure== | ||
2JOU is a [[Single protein]] structure | 2JOU is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2a2h 2a2h]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOU OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Walther, F J.]] | [[Category: Walther, F J.]] | ||
[[Category: Waring, A J.]] | [[Category: Waring, A J.]] | ||
[[Category: | [[Category: Lipid associated protein]] | ||
[[Category: | [[Category: Mini-b]] | ||
[[Category: | [[Category: Sp-b]] | ||
[[Category: | [[Category: Surface active protein]] | ||
[[Category: | [[Category: Surfactant protein b]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:07:43 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 06:07, 4 May 2008
NMR structure of Mini-B, an N-terminal- C-terminal construct from human Surfactant Protein-B (SP-B), in Hexafluoroisopropanol (HFIP)
Overview
Surfactant protein B (SP-B) is essential for normal lung surfactant function, which is in itself essential to life. However, the molecular basis for SP-B's activity is not understood and a high-resolution structure for SP-B has not been determined. Mini-B is a 34-residue peptide with internal disulfide linkages that is composed of the N- and C-terminal helical regions of SP-B. It has been shown to retain similar activity to full-length SP-B in certain in vitro and in vivo studies. We have used solution NMR to determine the structure of Mini-B in the presence of micelles composed of the anionic detergent sodium dodecyl sulfate (SDS). Under these conditions, Mini-B forms two alpha-helices connected by an unstructured loop. Mini-B possesses a strikingly amphipathic surface with a large positively charged patch on one face of the peptide and a large hydrophobic patch on the opposite face. A tryptophan side chain extends outward from the peptide in a position to interact with lipids at the polar/apolar interface. Interhelix interactions are stabilized by both disulfide bonds and by interleaving of hydrophobic side chains from the two helices.
About this Structure
2JOU is a Single protein structure. This structure supersedes the now removed PDB entry 2a2h. Full crystallographic information is available from OCA.
Reference
Structure of mini-B, a functional fragment of surfactant protein B, in detergent micelles., Sarker M, Waring AJ, Walther FJ, Keough KM, Booth V, Biochemistry. 2007 Oct 2;46(39):11047-56. Epub 2007 Sep 11. PMID:17845058 Page seeded by OCA on Sun May 4 09:07:43 2008
