Ligands bind to Sortilin in the tunnel of a ten-bladed β-propeller domain
EM Quistgaard, P Madsen, MK Grøftehauge… - Nature structural & …, 2009 - nature.com
Nature structural & molecular biology, 2009•nature.com
The structure of the Sortilin ectodomain in complex with neurotensin has been determined at
2-Å resolution, revealing that the C-terminal part of neurotensin binds in the tunnel of a ten-
bladed β-propeller domain. Binding competition studies suggest that additional binding
sites, for example, for the prodomain of nerve growth factor-β, are present in the tunnel and
that competition for binding relates to the restricted space inside the propeller.
2-Å resolution, revealing that the C-terminal part of neurotensin binds in the tunnel of a ten-
bladed β-propeller domain. Binding competition studies suggest that additional binding
sites, for example, for the prodomain of nerve growth factor-β, are present in the tunnel and
that competition for binding relates to the restricted space inside the propeller.
Abstract
The structure of the Sortilin ectodomain in complex with neurotensin has been determined at 2-Å resolution, revealing that the C-terminal part of neurotensin binds in the tunnel of a ten-bladed β-propeller domain. Binding competition studies suggest that additional binding sites, for example, for the prodomain of nerve growth factor-β, are present in the tunnel and that competition for binding relates to the restricted space inside the propeller.
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