2FHW
Solution structure of human relaxin-3
2FHW の概要
エントリーDOI | 10.2210/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 | |
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: 16365033DOI: 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
検証レポート(詳細版)をダウンロード