3K24

Crystal structure of mature apo-Cathepsin L C25A mutant in complex with Gln-Leu-Ala peptide

3K24 の概要

• エントリーDOI: 10.2210/pdb3k24/pdb
• 関連するPDBエントリー: 3IV2
• 分子名称: Cathepsin L1, H3 peptide, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-6)-beta-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: co-crystal, substrate, protease, structural genomics, structural genomics consortium, sgc, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 50315.26

構造登録者

Adams-Cioaba, M.A.,Krupa, J.C.,Mort, J.S.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2009-09-29, 公開日: 2010-03-23, 最終更新日: 2024-10-16)

主引用文献

Adams-Cioaba, M.A.,Krupa, J.C.,Xu, C.,Mort, J.S.,Min, J.
Structural basis for the recognition and cleavage of histone H3 by cathepsin L.
Nat Commun, 2:197-197, 2011

PubMed Abstract: Proteolysis of eukaryotic histone tails has emerged as an important factor in the modulation of cell-cycle progression and cellular differentiation. The recruitment of lysosomal cathepsin L to the nucleus where it mediates proteolysis of the mouse histone H3 tail has been described recently. Here, we report the three-dimensional crystal structures of a mature, inactive mutant of human cathepsin L alone and in complex with a peptide derived from histone H3. Canonical substrate-cathepsin L interactions are observed in the complex between the protease and the histone H3 peptide. Systematic analysis of the impact of posttranslational modifications at histone H3 on substrate selectivity suggests cathepsin L to be highly accommodating of all modified peptides. This is the first report of cathepsin L-histone H3 interaction and the first structural description of cathepsin L in complex with a substrate.

PubMed: 21326229
DOI: 10.1038/ncomms1204

実験手法

X-RAY DIFFRACTION (2.5 Å)