2jou
From Proteopedia
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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)
Contents |
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.
Disease
Known disease associated with this structure: Surfactant metabolism dysfunction, pulmonary, 1 OMIM:[178640]
About this Structure
2JOU is a Single protein structure of sequence from [1]. 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 Thu Mar 20 17:43:41 2008
