A model for the structure of a homodimeric prohormone: the precursor to the locust neuropeptide AKH I.
We have determined the structure in solution of a homodimeric protein that is a precursor to the locust neuropeptide adipokinetic hormone I using nuclear magnetic resonance spectroscopy. This precursor, called P1, is comprised of two 41 residue strands joined by a single inter-chain disulphide at Cys39. We have also determined the structure of an end product of P1 processing, called APRP1; this is a homodimer comprised of residues 14-41 of P1. Nuclear Overhauser Effect (nOe) data indicate that in both P1 and APRP1, residues 22-37 (numbered with respect to P1) form pairs of alpha-helices, with no evidence for any other secondary structure.
Horne
T J
TJ
Department of Biochemistry, University of Oxford, England.
Doak
D G
DG
Rayne
R C
RC
Balacco
G
G
O'Shea
M
M
Campbell
I D
ID
D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D007301:Insect Hormones / Q000096:biosynthesis / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011498:Protein Precursors / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary
D007301:Insect Hormones; D011498:Protein Precursors; C014956:adipokinetic hormone (locust)