1f0j
From Proteopedia
| |||||||
| , resolution 1.77Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | 3',5'-cyclic-nucleotide phosphodiesterase, with EC number 3.1.4.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 4B2B
Overview
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.
About this Structure
1F0J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity., Xu RX, Hassell AM, Vanderwall D, Lambert MH, Holmes WD, Luther MA, Rocque WJ, Milburn MV, Zhao Y, Ke H, Nolte RT, Science. 2000 Jun 9;288(5472):1822-5. PMID:10846163
Page seeded by OCA on Thu Mar 20 11:02:43 2008
