spacer
spacer

PDBsum entry 1spf

Go to PDB code: 
Top Page protein links
Lipoprotein(surface film) PDB id
1spf
Contents
Protein chain
35 a.a.

References listed in PDB file
Key reference
Title The nmr structure of the pulmonary surfactant-Associated polypeptide sp-C in an apolar solvent contains a valyl-Rich alpha-Helix.
Authors J.Johansson, T.Szyperski, T.Curstedt, K.Wüthrich.
Ref. Biochemistry, 1994, 33, 6015-6023. [DOI no: 10.1021/bi00185a042]
PubMed id 8180229
Abstract
The nuclear magnetic resonance (NMR) structure of the pulmonary surfactant-associated lipoplypeptide C (SP-C) was determined in a mixed solvent of C2H3Cl/C2H3OH/ 1 M HCl 32:64:5 (v/v). Sequence-specific 1H NMR assignments and the collection of conformational constraints were achieved with two-dimensional 1H NMR, and the structure was calculated with the distance geometry program DIANA. The root mean square deviations for the well-defined polypeptide segment of residues 9-34 calculated for the 20 best energy-minimized DIANA conformers relative to their mean are 0.5 and 1.3 A for the polypeptide backbone atoms N, C alpha, and C', and for all heavy atoms, respectively. The 35-residue polypeptide chain of SP-C forms an alpha-helix between positions 9 and 34, which includes two segments of seven and four consecutive valyls that are separated by a single leucyl residue. The N-terminal hexapeptide segment, which includes two palmitoylcysteinyls, is flexibly disordered. The length of the alpha-helix is about 37 A, and the helical segment of residues 13-28, which contains exclusively aliphatic residues with branched side chains, is 23-A long and about 10 A in diameter. The alpha-helix is outstandingly regular, with virtually identical chi 1 angles for all valyl residues. The observation of a helical structure of SP-C was rather unexpected, considering that Val is generally underrepresented in alpha-helices, and it provides intriguing novel insights into the structural basis of SP-C functions as well as into general structural aspects of protein-lipid interactions in biological membranes.
Secondary reference #1
Title Size and structure of the hydrophobic low molecular weight surfactant-Associated polypeptide.
Authors J.Johansson, T.Curstedt, B.Robertson, H.Jörnvall.
Ref. Biochemistry, 1988, 27, 3544-3547. [DOI no: 10.1021/bi00410a002]
PubMed id 3408709
Full text Abstract
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer