1SS6
Solution structure of SEP domain from human p47
1SS6 の概要
エントリーDOI | 10.2210/pdb1ss6/pdb |
NMR情報 | BMRB: 6189 |
分子名称 | NSFL1 cofactor p47 (1 entity in total) |
機能のキーワード | nmr; p47; sep, signaling protein |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Nucleus (By similarity): Q9UNZ2 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 11367.58 |
構造登録者 | Soukenik, M.,Leidert, M.,Sievert, V.,Buessow, K.,Leitner, D.,Labudde, D.,Ball, L.J.,Oschkinat, H. (登録日: 2004-03-23, 公開日: 2004-11-09, 最終更新日: 2024-05-22) |
主引用文献 | Soukenik, M.,Diehl, A.,Leidert, M.,Sievert, V.,Buessow, K.,Leitner, D.,Labudde, D.,Ball, L.J.,Lechner, A.,Nagler, D.K.,Oschkinat, H. The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L FEBS Lett., 576:358-362, 2004 Cited by PubMed Abstract: The solution structure of the human p47 SEP domain in a construct comprising residues G1-S2-p47(171-270) was determined by NMR spectroscopy. A structure-derived hypothesis about the domains' function was formulated and pursued in binding experiments with cysteine proteases. The SEP domain was found to be a reversible competitive inhibitor of cathepsin L with a Ki of 1.5 microM. The binding of G1-S2-p47(171-270) to cathepsin L was mapped by biochemical assays and the binding interface was investigated by NMR chemical shift perturbation experiments. PubMed: 15498563DOI: 10.1016/j.febslet.2004.09.037 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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