Secondary Structure Analysis of a Functional Construct of Caveolin-1 Reveals a Long C-Terminal Helix.
Caveolin-1 is an integral membrane protein that is the primary component of cell membrane invaginations called caveolae. While caveolin-1 is known to participate in a myriad of vital cellular processes, structural data on caveolin-1 of any kind is severely limited. In order to rectify this dearth, secondary structure analysis of a functional construct of caveolin-1, containing the intact C-terminal domain, was performed using NMR spectroscopy in lyso-myristoylphosphatidylglycerol micelles. Complete backbone assignments of caveolin-1 (residues 62-178) were made, and it was determined that residues 62-79 were dynamic; residues 89-107, 111-128, and 132-175 were helical; and residues 80-88, 108-110, and 129-131 represent unstructured breaks between the helices.
Department of Chemistry, Lehigh University, Bethlehem, Pennsylvania.
Sarah M
SM
Plucinsky
Department of Chemistry, Lehigh University, Bethlehem, Pennsylvania. Electronic address: kjg206@lehigh.edu.
Kerney Jebrell
KJ
Glover
D051242:Caveolin 1 / Q000737:chemistry* / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D010715:Phosphatidylglycerols / Q000737:chemistry; D017433:Protein Structure, Secondary; D013057:Spectrum Analysis
D051242:Caveolin 1; D008823:Micelles; D010715:Phosphatidylglycerols; C552372:lysomyristoylphosphatidylglycerol