1TTG
THE THREE-DIMENSIONAL STRUCTURE OF THE TENTH TYPE III MODULE OF FIBRONECTIN: AN INSIGHT INTO RGD-MEDIATED INTERACTIONS
1TTG の概要
エントリーDOI | 10.2210/pdb1ttg/pdb |
分子名称 | FIBRONECTIN (1 entity in total) |
機能のキーワード | glycoprotein |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Secreted, extracellular space, extracellular matrix: P02751 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 9947.06 |
構造登録者 | Main, A.L.,Harvey, T.S.,Baron, M.,Campbell, I.D. (登録日: 1993-07-14, 公開日: 1994-01-31, 最終更新日: 2024-05-01) |
主引用文献 | Main, A.L.,Harvey, T.S.,Baron, M.,Boyd, J.,Campbell, I.D. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell(Cambridge,Mass.), 71:671-678, 1992 Cited by PubMed Abstract: The solution structure of the tenth type III module of fibronectin has been determined using nuclear magnetic resonance techniques. The molecule has a fold similar to that of immunoglobulin domains, with seven beta strands forming two antiparallel beta sheets, which pack against each other. Both beta sheets contribute conserved hydrophobic residues to a compact core. The topology is more similar to that of domain 2 of CD4, PapD, and the extracellular domain of the human growth hormone receptor than to that of immunoglobulin C domains. The module contains an Arg-Gly-Asp sequence known to be involved in cell adhesion. This tripeptide is solvent exposed and lies on a conformationally mobile loop between strands F and G, consistent with its cell adhesion function. PubMed: 1423622DOI: 10.1016/0092-8674(92)90600-H 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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