3FHI

Crystal structure of a complex between the catalytic and regulatory (RI{alpha}) subunits of PKA

「1U7E」から置き換えられました

3FHI の概要

• エントリーDOI: 10.2210/pdb3fhi/pdb
• 分子名称: cAMP-dependent protein kinase catalytic subunit alpha, cAMP-dependent protein kinase type I-alpha regulatory subunit, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: camp, camp dependent protein kinase, protein-protein complex, amp-pnp, protein kinase regulation, nucleotide binding, protein kinase activity, protein serine/threonine kinase activity, camp-dependent protein kinase activity, protein binding, atp binding, kinase activity, transferase activity, atp-binding, kinase, lipoprotein, myristate, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, transferase, camp-binding
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cytoplasm . Isoform 2: Cell projection, cilium, flagellum : P05132; Cell membrane : P00514
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58580.89

構造登録者

Kim, C. (登録日: 2008-12-09, 公開日: 2009-04-14, 最終更新日: 2024-10-30)

主引用文献

Kim, C.,Xuong, N.H.,Taylor, S.S.
Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA.
Science, 307:690-696, 2005

PubMed Abstract: The 2.0-angstrom structure of the cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) catalytic subunit bound to a deletion mutant of a regulatory subunit (RIalpha) defines a previously unidentified extended interface. The complex provides a molecular mechanism for inhibition of PKA and suggests how cAMP binding leads to activation. The interface defines the large lobe of the catalytic subunit as a stable scaffold where Tyr247 in the G helix and Trp196 in the phosphorylated activation loop serve as anchor points for binding RIalpha. These residues compete with cAMP for the phosphate binding cassette in RIalpha. In contrast to the catalytic subunit, RIalpha undergoes major conformational changes when the complex is compared with cAMP-bound RIalpha. The inhibitor sequence docks to the active site, whereas the linker, also disordered in free RIalpha, folds across the extended interface. The beta barrel of cAMP binding domain A, which is the docking site for cAMP, remains largely intact in the complex, whereas the helical subdomain undergoes major reorganization.

PubMed: 15692043
DOI: 10.1126/science.1104607

実験手法

X-RAY DIFFRACTION (2 Å)