Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain.
The structure of the Sortilin ectodomain in complex with neurotensin has been determined at 2-A resolution, revealing that the C-terminal part of neurotensin binds in the tunnel of a ten-bladed beta-propeller domain. Binding competition studies suggest that additional binding sites, for example, for the prodomain of nerve growth factor-beta, are present in the tunnel and that competition for binding relates to the restricted space inside the propeller.
Quistgaard
Esben M
EM
MIND Centre, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK 8000 Arhus C, Denmark.
Madsen
Peder
P
Grøftehauge
Morten K
MK
Nissen
Poul
P
Petersen
Claus M
CM
Thirup
Søren S
SS
D033942:Adaptor Proteins, Vesicular Transport / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D017209:Apoptosis; D001665:Binding Sites; D008024:Ligands; D008322:Mammals; D008958:Models, Molecular; D009474:Neurons / Q000502:physiology; D009496:Neurotensin / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D000099183:Sortilin
D033942:Adaptor Proteins, Vesicular Transport; D008024:Ligands; D009496:Neurotensin; D000099183:Sortilin