3A7Q

Structural basis for specific recognition of reelin by its receptors

Summary for 3A7Q

• Entry DOI: 10.2210/pdb3a7q/pdb
• Descriptor: Reelin, Low-density lipoprotein receptor-related protein 8, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: signaling protein
• Biological source: Mus musculus (mouse); More
• Cellular location: Secreted, extracellular space, extracellular matrix: Q60841; Cell membrane ; Single-pass type I membrane protein : Q14114
• Total number of polymer chains: 2
• Total formula weight: 87753.35

Authors

Yasui, N.,Nogi, T.,Takagi, J. (deposition date: 2009-10-01, release date: 2010-03-23, Last modification date: 2024-10-30)

Primary citation

Yasui, N.,Nogi, T.,Takagi, J.
Structural Basis for Specific Recognition of Reelin by Its Receptors
Structure, 18:320-331, 2010

PubMed Abstract: Apolipoprotein E receptor 2 (ApoER2) and very-low-density lipoprotein receptor, members of the low-density lipoprotein receptor (LDLR) protein family, function as neuronal receptors for a secreted glycoprotein reelin during brain development. In both receptors, the first LDLR class A (LA1) module is sufficient to bind reelin. Analysis of a 2.6 A crystal structure of the reelin receptor-binding fragment in complex with the LA1 of ApoER2 revealed that Lys2467 of reelin is recognized by both a conserved Trp residue and calcium-coordinating acidic residues from LA1, which together with Lys2360 plays a critical role in the interaction. This "double-Lys" recognition mode is, in fact, shared among other LDLR family proteins in ligand binding. The interface between reelin and LA1 covers a small surface area of approximately 350 A(2) on each side, which ensures a stable complex formation under physiological conditions. An examination of structure-guided mutagenesis on interface residues revealed key features of this interaction.

PubMed: 20223215
DOI: 10.1016/j.str.2010.01.010

Experimental method

X-RAY DIFFRACTION (2.6 Å)