2CH9

Crystal structure of dimeric human cystatin F

2CH9 の概要

• エントリーDOI: 10.2210/pdb2ch9/pdb
• 分子名称: CYSTATIN F, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: inhibitor, cysteine protease inhibitor, glycoprotein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16433.33

構造登録者

Schuettelkopf, A.W.,van Aalten, D.M.F. (登録日: 2006-03-13, 公開日: 2006-04-04, 最終更新日: 2024-10-23)

主引用文献

Schuttelkopf, A.W.,Hamilton, G.,Watts, C.,Van Aalten, D.M.F.
Structural Basis of Reduction-Dependent Activation of Human Cystatin F.
J.Biol.Chem., 281:16570-, 2006

PubMed Abstract: Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase. Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes. It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile. We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state. The two monomers interact in a fashion not seen before for cystatins or cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation. Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.

PubMed: 16601115
DOI: 10.1074/JBC.M601033200

実験手法

X-RAY DIFFRACTION (2.1 Å)