1WNH

Crystal structure of mouse Latexin (tissue carboxypeptidase inhibitor)

1WNH の概要

• エントリーDOI: 10.2210/pdb1wnh/pdb
• 分子名称: Latexin (2 entities in total)
• 機能のキーワード: bi-cystatin fold, cis-proline, hydrolase inhibitor, hydrolase inhibitor
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm (Probable): P70202
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25838.11

構造登録者

Aagaard, A.,Listwan, P.,Cowieson, N.,Huber, T.,Ravasi, T.,Wells, C.A.,Flanagan, J.U.,Hume, D.A.,Kobe, B.,Martin, J.L. (登録日: 2004-08-04, 公開日: 2005-02-15, 最終更新日: 2024-03-13)

主引用文献

Aagaard, A.,Listwan, P.,Cowieson, N.,Huber, T.,Ravasi, T.,Wells, C.A.,Flanagan, J.U.,Kellie, S.,Hume, D.A.,Kobe, B.,Martin, J.L.
An Inflammatory Role for the Mammalian Carboxypeptidase Inhibitor Latexin: Relationship to Cystatins and the Tumor Suppressor TIG1
Structure, 13:309-317, 2005

PubMed Abstract: Latexin, the only known mammalian carboxypeptidase inhibitor, has no detectable sequence similarity with plant and parasite inhibitors, but it is related to a human putative tumor suppressor protein, TIG1. Latexin is expressed in the developing brain, and we find that it plays a role in inflammation, as it is expressed at high levels and is inducible in macrophages in concert with other protease inhibitors and potential protease targets. The crystal structure of mouse latexin, solved at 1.83 A resolution, shows no structural relationship with other carboxypeptidase inhibitors. Furthermore, despite a lack of detectable sequence duplication, the structure incorporates two topologically analogous domains related by pseudo two-fold symmetry. Surprisingly, these domains share a cystatin fold architecture found in proteins that inhibit cysteine proteases, suggesting an evolutionary and possibly functional relationship. The structure of the tumor suppressor protein TIG1 was modeled, revealing its putative membrane binding surface.

PubMed: 15698574
DOI: 10.1016/j.str.2004.12.013

実験手法

X-RAY DIFFRACTION (1.83 Å)