1F0J

CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 4B2B

Summary for 1F0J

• Entry DOI: 10.2210/pdb1f0j/pdb
• Descriptor: PHOSPHODIESTERASE 4B, ZINC ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: pde phosphodiesterase, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 87195.35

Authors

Xu, R.X.,Hassell, A.M.,Vanderwall, D.,Lambert, M.H.,Holmes, W.D.,Luther, M.A.,Rocque, W.J.,Milburn, M.V.,Zhao, Y.,Ke, H.,Nolte, R.T. (deposition date: 2000-05-16, release date: 2000-07-26, Last modification date: 2024-02-07)

Primary citation

Xu, R.X.,Hassell, A.M.,Vanderwall, D.,Lambert, M.H.,Holmes, W.D.,Luther, M.A.,Rocque, W.J.,Milburn, M.V.,Zhao, Y.,Ke, H.,Nolte, R.T.
Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity.
Science, 288:1822-1825, 2000

PubMed Abstract: Cyclic nucleotides are second messengers that are essential in vision, muscle contraction, neurotransmission, exocytosis, cell growth, and differentiation. These molecules are degraded by a family of enzymes known as phosphodiesterases, which serve a critical function by regulating the intracellular concentration of cyclic nucleotides. We have determined the three-dimensional structure of the catalytic domain of phosphodiesterase 4B2B to 1.77 angstrom resolution. The active site has been identified and contains a cluster of two metal atoms. The structure suggests the mechanism of action and basis for specificity and will provide a framework for structure-assisted drug design for members of the phosphodiesterase family.

PubMed: 10846163
DOI: 10.1126/science.288.5472.1822

Experimental method

X-RAY DIFFRACTION (1.77 Å)