1H, 15N and 13C resonance assignment of darcin, a mouse major urinary protein.
Darcin is an important lipocalin of the urinary MUP family. These beta-barrel structures differ subtly in sequence and function and facilitate communication between members of the mouse population via scent marks. Polymorphism within the family has led to the hypothesis that individual MUPs can also contribute to social and physiological information of the scent owner and thus demonstrates the necessity for structural investigation of these variations. Using conventional triple resonance experiments, (1)H (15)N and (13)C assignment of recombinant N terminal hexa-histidine tagged Darcin has been achieved. The corresponding chemical shifts have been deposited in the BioMagResBank; Accession No. 16840.
Phelan
Marie M
MM
NMR Centre for Structural Biology, Biological Sciences, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK.
McLean
Lynn
L
Simpson
Deborah M
DM
Hurst
Jane L
JL
Beynon
Robert J
RJ
Lian
Lu-Yun
LY
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D006859:Hydrogen; D036341:Intercellular Signaling Peptides and Proteins; D051379:Mice; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
D002247:Carbon Isotopes; D036341:Intercellular Signaling Peptides and Proteins; C555029:Mup20 protein, mouse; D009587:Nitrogen Isotopes; D011506:Proteins; D011994:Recombinant Proteins; C035737:major urinary proteins; D006859:Hydrogen