Modeling the Primary Hormone-Binding Site of RXFP1 and RXFP2

The primary binding sites of the relaxin and insulin‐like peptide 3 (INSL3) receptors, RXFP1 and RXFP2, are found within the leucine‐rich repeats (LRRs) of the ectodomains. Specific B‐chain residues in the peptides interact with residues in the inner β‐sheets of the LRRs of the receptors. Relaxin bi...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 2009-04, Vol.1160 (1), p.74-77
Main Authors: Scott, Daniel J., Tregear, Geoffrey W., Bathgate, Ross A. D.
Format: Article
Language:English
Subjects:
Binding Sites
GPCR
Humans
LDL-A
LGR7
LGR8
Models, Molecular
molecular modeling
Protein Binding
Protein Structure, Tertiary
Receptors, G-Protein-Coupled - chemistry
Receptors, G-Protein-Coupled - metabolism
Receptors, Peptide - chemistry
Receptors, Peptide - metabolism
Relaxin - chemistry
Relaxin - metabolism
RXFP1
RXFP2
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Summary:The primary binding sites of the relaxin and insulin‐like peptide 3 (INSL3) receptors, RXFP1 and RXFP2, are found within the leucine‐rich repeats (LRRs) of the ectodomains. Specific B‐chain residues in the peptides interact with residues in the inner β‐sheets of the LRRs of the receptors. Relaxin binds to RXFP2 with high affinity, although INSL3 has a very poor affinity for RXFP1. In this paper we present evidence that relaxin binds to the LRRs of RXFP2 in a manner similar to INSL3 binding to its receptor. Additionally, we introduce a model of this binding interaction and compare it to an alternate model for relaxin–RXFP1 binding.
ISSN:0077-8923
1749-6632
DOI:10.1111/j.1749-6632.2009.03950.x