1NP8

18-k C-terminally trunucated small subunit of calpain

1NP8 の概要

• エントリーDOI: 10.2210/pdb1np8/pdb
• 分子名称: Calcium-dependent protease, small subunit, CADMIUM ION (3 entities in total)
• 機能のキーワード: dimer in solution, oligomer in crystal, hydrolase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm: Q64537
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38162.61

構造登録者

Leinala, E.K.,Arthur, J.S.,Grochulski, P.,Davies, P.L.,Elce, J.S.,Jia, Z. (登録日: 2003-01-17, 公開日: 2003-11-18, 最終更新日: 2024-02-14)

主引用文献

Leinala, E.K.,Arthur, J.S.,Grochulski, P.,Davies, P.L.,Elce, J.S.,Jia, Z.
A second binding site revealed by C-terminal truncation of calpain small subunit, a penta-EF-hand protein
PROTEINS: STRUCT.,FUNCT.,GENET., 53:649-655, 2003

PubMed Abstract: The subunits in calpain and in the related penta-EF-hand (PEF) proteins are bound through contacts between the unpaired EF-hand 5 from each subunit. To study subunit binding further, a tetra-EF-hand 18 kDa N- and C-terminally truncated form of the calpain small subunit was prepared (18k). This protein does not combine with the calpain large subunit to form active calpain, but forms homodimers in solution, as shown by ultracentrifugation. The X-ray structure of the 18k protein in the presence of cadmium was solved to a resolution of 2.0 A. The structure of the monomer is almost identical to the known structure of the calpain small subunit, but the 18k protein forms an oligomer in the crystal by the use of two binding sites. One of these sites is an artefact arising from the C-terminal truncation, but the other is a naturally occurring site that is fully exposed to water in intact purified calpain. The characteristics of this site suggest that it may be important in binding other protein modulators involved in the regulation of calpain and of PEF proteins.

PubMed: 14579356
DOI: 10.1002/prot.10453

実験手法

X-RAY DIFFRACTION (2 Å)