2I9B
Crystal structure of ATF-urokinase receptor complex
2I9B の概要
| エントリーDOI | 10.2210/pdb2i9b/pdb |
| 関連するPDBエントリー | 2I9A |
| 分子名称 | Urokinase-type plasminogen activator, Urokinase plasminogen activator surface receptor, beta-D-mannopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| 機能のキーワード | urokinase receptor, kringle domain, growth factor-like domain, hydrolase |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 192247.71 |
| 構造登録者 | |
| 主引用文献 | Barinka, C.,Parry, G.,Callahan, J.,Shaw, D.E.,Kuo, A.,Bdeir, K.,Cines, D.B.,Mazar, A.,Lubkowski, J. Structural basis of interaction between urokinase-type plasminogen activator and its receptor. J.Mol.Biol., 363:482-495, 2006 Cited by PubMed Abstract: Recent studies indicate that binding of the urokinase-type plasminogen activator (uPA) to its high-affinity receptor (uPAR) orchestrates uPAR interactions with other cellular components that play a pivotal role in diverse (patho-)physiological processes, including wound healing, angiogenesis, inflammation, and cancer metastasis. However, notwithstanding the wealth of biochemical data available describing the activities of uPAR, little is known about the exact mode of uPAR/uPA interactions or the presumed conformational changes that accompany uPA/uPAR engagement. Here, we report the crystal structure of soluble urokinase plasminogen activator receptor (suPAR), which contains the three domains of the wild-type receptor but lacks the cell-surface anchoring sequence, in complex with the amino-terminal fragment of urokinase-type plasminogen activator (ATF), at the resolution of 2.8 A. We report the 1.9 A crystal structure of free ATF. Our results provide a structural basis, represented by conformational changes induced in uPAR, for several published biochemical observations describing the nature of uPAR/uPA interactions and provide insight into mechanisms that may be responsible for the cellular responses induced by uPA binding. PubMed: 16979660DOI: 10.1016/j.jmb.2006.08.063 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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