1ITP
Solution Structure of POIA1
1ITP の概要
エントリーDOI | 10.2210/pdb1itp/pdb |
分子名称 | proteinase A inhibitor 1 (1 entity in total) |
機能のキーワード | inhibitor, propeptide, beta-alpha-beta, protein binding |
由来する生物種 | Pleurotus ostreatus (oyster mushroom) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 8331.24 |
構造登録者 | Sasakawa, H.,Yoshinaga, S.,Kojima, S.,Tamura, A. (登録日: 2002-01-23, 公開日: 2002-02-13, 最終更新日: 2023-12-27) |
主引用文献 | Sasakawa, H.,Yoshinaga, S.,Kojima, S.,Tamura, A. Structure of POIA1, a homologous protein to the propeptide of subtilisin: implication for protein foldability and the function as an intramolecular chaperone. J.Mol.Biol., 317:159-167, 2002 Cited by PubMed Abstract: Solution structure of POIA1 (Pleurotus ostreatus proteinase A inhibitor 1), which functions as an intramolecular chaperone and as an inhibitor to subtilisin, was determined. By making use of the fact that POIA1 is the only structured protein that shows homology to the propeptide of subtilisin, which is unstructured by itself, foldability of this protein was elucidated. It became clear that the evolutionarily conserved residues play two important roles, one for the maintenance of its own structure, and the other for the interaction with subtilisin. Structural softness and mutational tolerance contained in the POIA1 structure makes it an ideal material for designing a foldable protein. PubMed: 11916386DOI: 10.1006/jmbi.2002.5412 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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