Backbone and side-chain assignment of the lipidated and non-lipidated forms of the meningococcal outer membrane protein LP2086.
LP2086 is a lipidated outer membrane protein from Neisseria meningitidis that elicits bactericidal antibodies and represents a promising vaccine candidate against meningococcal infections. Here we report the backbone and side-chain assignment for two forms of LP2086: non-lipidated in aqueous buffer and the lipidated protein in micellar solution.
Mascioni
A
A
Wyeth Research, Structural Biology and Computational Chemistry, 200 Cambridge Park Drive, 02140, Cambridge, MA, USA. masci002@umn.edu
Jacob
J
J
Moy
F
F
Dilts
D
D
Fink
P
P
Malakian
K
K
Sigethy
S
S
Wen
Y
Y
Novikova
E
E
Zlotnick
G W
GW
Tsao
D H H
DH
D000595:Amino Acid Sequence; D000942:Antigens, Bacterial / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008563:Membrane Lipids / Q000737:chemistry*; D008823:Micelles; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D002247:Carbon Isotopes; D008563:Membrane Lipids; D008823:Micelles; D009587:Nitrogen Isotopes; D021122:Protein Subunits; D011522:Protons; C484699:factor H-binding protein, Neisseria meningitidis