1CM8

PHOSPHORYLATED MAP KINASE P38-GAMMA

Summary for 1CM8

• Entry DOI: 10.2210/pdb1cm8/pdb
• Descriptor: PHOSPHORYLATED MAP KINASE P38-GAMMA, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: p38-gamma, gamma, phosphorylation, map kinase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P53778
• Total number of polymer chains: 2
• Total formula weight: 85423.79

Authors

Bellon, S.,Fitzgibbon, M.J.,Fox, T.,Hsiao, H.M.,Wilson, K.P. (deposition date: 1999-05-17, release date: 2000-05-17, Last modification date: 2024-11-20)

Primary citation

Bellon, S.,Fitzgibbon, M.J.,Fox, T.,Hsiao, H.M.,Wilson, K.P.
The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation.
Structure Fold.Des., 7:1057-1065, 1999

PubMed Abstract: Mitogen-activated protein (MAP) kinases mediate the cellular response to stimuli such as pro-inflammatory cytokines and environmental stress. P38gamma is a new member of the MAP kinase family, and is expressed at its highest levels in skeletal muscle. P38gamma is 63% identical in sequence to P38alpha. The structure of P38alpha MAP kinase has been determined in the apo, unphosphorylated, inactive form. The structures of apo unphosphorylated ERK2, a related MAP kinase, and apo phosphorylated ERK2 have also been determined.

PubMed: 10508788
DOI: 10.1016/S0969-2126(99)80173-7

Experimental method

X-RAY DIFFRACTION (2.4 Å)