Journal article

Defining the LGR8 residues involved in binding insulin-like peptide 3

Daniel J Scott, Tracey N Wilkinson, Suode Zhang, Tania Ferraro, John D Wade, Geoffrey W Tregear, Ross AD Bathgate

MOLECULAR ENDOCRINOLOGY | ENDOCRINE SOC | Published : 2007

Abstract

The peptide hormone insulin-like peptide 3 (INSL3) is essential for testicular descent and has been implicated in the control of adult fertility in both sexes. The human INSL3 receptor leucine-rich repeat-containing G protein-coupled receptor 8 (LGR8) binds INSL3 and relaxin with high affinity, whereas the relaxin receptor LGR7 only binds relaxin. LGR7 and LGR8 bind their ligands within the 10 leucine-rich repeats (LRRs) that comprise the majority of their ectodomains. To define the primary INSL3 binding site in LGR8, its LRRs were first modeled on the crystal structure of the Nogo receptor (NgR) and the most likely binding surface identified. Multiple sequence alignment of this surface reve..

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