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2FHW

Solution structure of human relaxin-3

2FHW の概要
エントリーDOI10.2210/pdb2fhw/pdb
分子名称Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7) (2 entities in total)
機能のキーワードinsulin/relaxin super-family fold, signaling protein
細胞内の位置Secreted: Q8WXF3 Q8WXF3
タンパク質・核酸の鎖数2
化学式量合計5513.43
構造登録者
Rosengren, K.J.,Craik, D.J. (登録日: 2005-12-27, 公開日: 2006-01-24, 最終更新日: 2022-03-09)
主引用文献Rosengren, K.J.,Lin, F.,Bathgate, R.A.,Tregear, G.W.,Daly, N.L.,Wade, J.D.,Craik, D.J.
Solution structure and novel insights into the determinants of the receptor specificity of human relaxin-3.
J.Biol.Chem., 281:5845-5851, 2006
Cited by
PubMed Abstract: Relaxin-3 is the most recently discovered member of the relaxin family of peptide hormones. In contrast to relaxin-1 and -2, whose main functions are associated with pregnancy, relaxin-3 is involved in neuropeptide signaling in the brain. Here, we report the solution structure of human relaxin-3, the first structure of a relaxin family member to be solved by NMR methods. Overall, relaxin-3 adopts an insulin-like fold, but the structure differs crucially from the crystal structure of human relaxin-2 near the B-chain terminus. In particular, the B-chain C terminus folds back, allowing Trp(B27) to interact with the hydrophobic core. This interaction partly blocks the conserved RXXXRXXI motif identified as a determinant for the interaction with the relaxin receptor LGR7 and may account for the lower affinity of relaxin-3 relative to relaxin for this receptor. This structural feature is likely important for the activation of its endogenous receptor, GPCR135.
PubMed: 16365033
DOI: 10.1074/jbc.M511210200
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2fhw
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件を2024-10-30に公開中

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