2Y4T

Crystal structure of the human co-chaperone P58(IPK)

2Y4T の概要

• エントリーDOI: 10.2210/pdb2y4t/pdb
• 関連するPDBエントリー: 2Y4U
• 分子名称: DNAJ HOMOLOG SUBFAMILY C MEMBER 3 (2 entities in total)
• 機能のキーワード: chaperone, endoplasmic reticulum, protein folding, tetratricopeptiderepeat, j domain, unfolded protein response
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Endoplasmic reticulum (By similarity): Q13217
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 155840.51

構造登録者

Svard, M.,Biterova, E.I.,Bourhis, J.-M.,Guy, J.E. (登録日: 2011-01-10, 公開日: 2011-08-10, 最終更新日: 2024-11-06)

主引用文献

Svard, M.,Biterova, E.I.,Bourhis, J.-M.,Guy, J.E.
The Crystal Structure of the Human Co-Chaperone P58Ipk
Plos One, 6:22337-, 2011

PubMed Abstract: P58(IPK) is one of the endoplasmic reticulum- (ER-) localised DnaJ (ERdj) proteins which interact with the chaperone BiP, the mammalian ER ortholog of Hsp70, and are thought to contribute to the specificity and regulation of its diverse functions. P58(IPK), expression of which is upregulated in response to ER stress, has been suggested to act as a co-chaperone, binding un- or misfolded proteins and delivering them to BiP. In order to give further insights into the functions of P58(IPK), and the regulation of BiP by ERdj proteins, we have determined the crystal structure of human P58(IPK) to 3.0 Å resolution using a combination of molecular replacement and single wavelength anomalous diffraction. The structure shows the human P58(IPK) monomer to have a very elongated overall shape. In addition to the conserved J domain, P58(IPK) contains nine N-terminal tetratricopeptide repeat motifs, divided into three subdomains of three motifs each. The J domain is attached to the C-terminal end via a flexible linker, and the structure shows the conserved Hsp70-binding histidine-proline-aspartate (HPD) motif to be situated on the very edge of the elongated protein, 100 Å from the putative binding site for unfolded protein substrates. The residues that comprise the surface surrounding the HPD motif are highly conserved in P58(IPK) from other organisms but more varied between the human ERdj proteins, supporting the view that their regulation of different BiP functions is facilitated by differences in BiP-binding.

PubMed: 21799829
DOI: 10.1371/JOURNAL.PONE.0022337

実験手法

X-RAY DIFFRACTION (3 Å)