1SPF

THE NMR STRUCTURE OF THE PULMONARY SURFACTANT-ASSOCIATED POLYPEPTIDE SP-C IN AN APOLAR SOLVENT CONTAINS A VALYL-RICH ALPHA-HELIX

1SPF の概要

• エントリーDOI: 10.2210/pdb1spf/pdb
• 分子名称: PULMONARY SURFACTANT-ASSOCIATED POLYPEPTIDE C (1 entity in total)
• 機能のキーワード: lipoprotein(surface film)
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted, extracellular space, surface film: P15785
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3712.86

構造登録者

Johansson, J.,Szyperski, T.,Curstedt, T.,Wuthrich, K. (登録日: 1994-09-26, 公開日: 1994-12-20, 最終更新日: 2024-05-22)

主引用文献

Johansson, J.,Szyperski, T.,Curstedt, T.,Wuthrich, K.
The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix.
Biochemistry, 33:6015-6023, 1994

PubMed 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.

PubMed: 8180229
DOI: 10.1021/bi00185a042

実験手法

SOLUTION NMR