1E9K
The structure of the RACK1 interaction sites located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5.
Summary for 1E9K
Entry DOI | 10.2210/pdb1e9k/pdb |
Descriptor | cAMP-specific 3',5'-cyclic phosphodiesterase 4D (1 entity in total) |
Functional Keywords | hydrolase, camp-specific phosphodiesterase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 4430.99 |
Authors | Bolger, G.B.,Smith, K.J.,McCahill, A.,Hyde, E.I.,Steele, M.R.,Houslay, M.D. (deposition date: 2000-10-20, release date: 2001-10-18, Last modification date: 2018-06-20) |
Primary citation | Smith, K.J.,Baillie, G.S.,Hyde, E.I.,Li, X.,Houslay, T.M.,McCahill, A.,Dunlop, A.J.,Bolger, G.B.,Klussmann, E.,Adams, D.R.,Houslay, M.D. 1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1. Cell. Signal., 19:2612-2624, 2007 Cited by PubMed: 17900862DOI: 10.1016/j.cellsig.2007.08.015 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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