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Comparative structural analysis of the binding domain of follicle stimulating hormone receptor
Author(s) -
Fan Qing R.,
Hendrickson Wayne A.
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21937
Subject(s) - leucine rich repeat , protein structure , receptor , biology , follicle stimulating hormone receptor , protein domain , chemistry , hormone , microbiology and biotechnology , follicle stimulating hormone , biochemistry , luteinizing hormone , gene
Proteins with leucine‐rich repeats (LRRs) specialize in mediating protein–protein interactions. The hormone binding portion of the receptor for follicle stimulating hormone (FSH) is an LRR protein by sequence, and the crystal structure of this domain from human FSH receptor in a complex with FSH shows that it does indeed have an LRR structure. It differs from other LRR domains, however, in being an all‐β protein composed of highly irregular repeats and having only slight overall curvature. Despite these distinctions and a superficial resemblance to β‐helical proteins, the binding domain of FSH receptor clearly is an LRR protein. The structure does consist of two parts with distinctively different curvatures. Comparison with the structures of other LRR‐containing proteins shows a correlation between curvature and main‐chain hydrogen bonding pattern of the parallel β‐sheet. The hormone‐binding site is located at the concave surface of the receptor structure, a feature common to proteins with LRR motifs. Analysis of the ligand‐binding site of LRR‐containing proteins reveals that they generally utilize extensive interface area and a large number of charged residues to facilitate high‐affinity protein‐protein interactions. Proteins 2008. © 2008 Wiley‐Liss, Inc.