6ZTK

Crystal structure of Mialostatin, a gut cystatin from the hard tick Ixodes ricinus

6ZTK の概要

• エントリーDOI: 10.2210/pdb6ztk/pdb
• 分子名称: Mialostatin, FRAGMENT OF TRITON X-100, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: cystatin, protease inhibitor, ixodes ricinus, tick, hydrolase inhibitor, protein binding
• 由来する生物種: Ixodes ricinus (Common tick)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32531.17

構造登録者

Busa, M.,Rezacova, P.,Mares, M. (登録日: 2020-07-20, 公開日: 2021-06-02, 最終更新日: 2024-10-23)

主引用文献

Kotal, J.,Busa, M.,Urbanova, V.,Rezacova, P.,Chmelar, J.,Langhansova, H.,Sojka, D.,Mares, M.,Kotsyfakis, M.
Mialostatin, a Novel Midgut Cystatin from Ixodes ricinus Ticks: Crystal Structure and Regulation of Host Blood Digestion.
Int J Mol Sci, 22:-, 2021

PubMed Abstract: The hard tick is a vector of Lyme disease and tick-borne encephalitis. Host blood protein digestion, essential for tick development and reproduction, occurs in tick midgut digestive cells driven by cathepsin proteases. Little is known about the regulation of the digestive proteolytic machinery of . Here we characterize a novel cystatin-type protease inhibitor, mialostatin, from the midgut. Blood feeding rapidly induced mialostatin expression in the gut, which continued after tick detachment. Recombinant mialostatin inhibited a number of digestive cysteine cathepsins, with the greatest potency observed against cathepsin L isoforms, with which it co-localized in midgut digestive cells. The crystal structure of mialostatin was determined at 1.55 Å to explain its unique inhibitory specificity. Finally, mialostatin effectively blocked in vitro proteolysis of blood proteins by midgut cysteine cathepsins. Mialostatin is likely to be involved in the regulation of gut-associated proteolytic pathways, making midgut cystatins promising targets for tick control strategies.

PubMed: 34065290
DOI: 10.3390/ijms22105371

実験手法

X-RAY DIFFRACTION (1.55 Å)