1PHK

TWO STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHORYLASE, KINASE: AN ACTIVE PROTEIN KINASE COMPLEXED WITH NUCLEOTIDE, SUBSTRATE-ANALOGUE AND PRODUCT

1PHK の概要

• エントリーDOI: 10.2210/pdb1phk/pdb
• 分子名称: PHOSPHORYLASE KINASE, MANGANESE (II) ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: glycogen metabolism, transferase, serine/threonine-protein, kinase, atp-binding, calmodulin-binding
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34933.35

構造登録者

Owen, D.J.,Noble, M.E.M.,Garman, E.F.,Papageorgiou, A.C.,Johnson, L.N. (登録日: 1996-03-15, 公開日: 1996-08-17, 最終更新日: 2024-02-14)

主引用文献

Owen, D.J.,Noble, M.E.,Garman, E.F.,Papageorgiou, A.C.,Johnson, L.N.
Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product.
Structure, 3:467-482, 1995

PubMed Abstract: Control of intracellular events by protein phosphorylation is promoted by specific protein kinases. All the known protein kinase possess a common structure that defines a catalytically competent entity termed the 'kinase catalytic core'. Within this common structural framework each kinase displays its own unique substrate specificity, and a regulatory mechanism that may be modulated by association with other proteins. Structural studies of phosphorylase kinase (Phk), the major substrate of which is glycogen phosphorylase, may be expected to shed light on its regulation.

PubMed: 7663944
DOI: 10.1016/S0969-2126(01)00180-0

実験手法

X-RAY DIFFRACTION (2.2 Å)