Structure and Dynamics of the Myristoyl Lipid Modification of Src Peptides Determined by 2H Solid-State NMR Spectroscopy
AUTOR(ES)
Scheidt, Holger A.
FONTE
The Biophysical Society
RESUMO
Lipid modifications of proteins are widespread in nature and play an important role in numerous biological processes. The nonreceptor tyrosine kinase Src is equipped with an N-terminal myristoyl chain and a cluster of basic amino acids for the stable membrane association of the protein. We used 2H NMR spectroscopy to investigate the structure and dynamics of the myristoyl chain of myr-Src(2–19), and compare them with the hydrocarbon chains of the surrounding phospholipids in bilayers of varying surface potentials and chain lengths. The myristoyl chain of Src was well inserted in all bilayers investigated. In zwitterionic 1,2-dimyristoyl-sn-glycero-3-phosphocholine membranes, the myristoyl chain of Src was significantly longer and appears “stiffer” than the phospholipid chains. This can be explained by an equilibrium between the attraction attributable to the insertion of the myristoyl chain and the Born repulsion. In a 1,2-dimyristoyl-sn-glycero-3-phosphocholine/1,2-dimyristoyl-sn-glycero-3-[phospho-L-serine] membrane, where attractive electrostatic interactions come into play, the differences between the peptide and the phospholipid chain lengths were attenuated, and the molecular dynamics of all lipid chains were similar. In a much thicker 1,2-dipalmitoyl-sn-glycero-3-phosphocholine/1,2-dipalmitoyl-sn-glycero-3-[phospho-L-serine]/cholesterol membrane, the length of the myristoyl chain of Src was elongated nearly to its maximum, and the order parameters of the Src chain were comparable to those of the surrounding membrane.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2711427Documentos Relacionados
- Characterization of leucine side-chain reorientation in collagen-fibrils by solid-state 2H NMR.
- Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy
- Model of interaction between a cardiotoxin and dimyristoylphosphatidic acid bilayers determined by solid-state 31P NMR spectroscopy.
- De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy
- Protein dynamics by solid-state NMR: aromatic rings of the coat protein in fd bacteriophage.