1POE

STRUCTURES OF FREE AND INHIBITED HUMAN SECRETORY PHOSPHOLIPASE A2 FROM INFLAMMATORY EXUDATE

1POE の概要

• エントリーDOI: 10.2210/pdb1poe/pdb
• 分子名称: PHOSPHOLIPASE A2, CALCIUM ION, 1-O-OCTYL-2-HEPTYLPHOSPHONYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Peripheral membrane protein: P14555
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29029.38

構造登録者

Scott, D.L.,White, S.P.,Sigler, P.B. (登録日: 1992-09-07, 公開日: 1993-10-31, 最終更新日: 2024-10-16)

主引用文献

Scott, D.L.,White, S.P.,Browning, J.L.,Rosa, J.J.,Gelb, M.H.,Sigler, P.B.
Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate.
Science, 254:1007-1010, 1991

PubMed Abstract: Phospholipase A2 (PLA2) participates in a wide range of cellular processes including inflammation and transmembrane signaling. A human nonpancreatic secretory PLA2 (hnps-PLA2) has been identified that is found in high concentrations in the synovial fluid of patients with rheumatoid arthritis and in the plasma of patients with septic shock. This enzyme is secreted from certain cell types in response to the proinflammatory cytokines, tumor necrosis factor or interleukin-1. The crystal structures of the calcium-bound form of this enzyme have been determined at physiological pH both in the presence [2.1 angstrom (A) resolution] and absence (2.2 A resolution) of a transition-state analogue. Although the critical features that suggest the chemistry of catalysis are identical to those inferred from the crystal structures of other extracellular PLA2s, the shape of the hydrophobic channel of hnps-PLA2 is uniquely modulated by substrate binding.

PubMed: 1948070

実験手法

X-RAY DIFFRACTION (2.1 Å)