2JOU
NMR structure of Mini-B, an N-terminal- C-terminal construct from human Surfactant Protein-B (SP-B), in Hexafluoroisopropanol (HFIP)
Replaces: 2A2HSummary for 2JOU
| Entry DOI | 10.2210/pdb2jou/pdb |
| Related | 1RG3 1RG4 |
| NMR Information | BMRB: 6741 |
| Descriptor | Pulmonary surfactant-associated protein B (1 entity in total) |
| Functional Keywords | mini-b, sp-b, surfactant protein b, lipid associated protein, surface active protein |
| Cellular location | Secreted, extracellular space, surface film: P07988 |
| Total number of polymer chains | 1 |
| Total formula weight | 3934.02 |
| Authors | Booth, V.,Sarker, M.,Keough, K.M.W.,Waring, A.J.,Walther, F.J. (deposition date: 2007-03-26, release date: 2007-04-10, Last modification date: 2023-12-20) |
| Primary citation | Sarker, M.,Waring, A.J.,Walther, F.J.,Keough, K.M.,Booth, V. Structure of mini-B, a functional fragment of surfactant protein B, in detergent micelles Biochemistry, 46:11047-11056, 2007 Cited by PubMed Abstract: 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. PubMed: 17845058DOI: 10.1021/bi7011756 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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