2NPQ
A Novel Lipid Binding Site in the p38 alpha MAP Kinase
Summary for 2NPQ
| Entry DOI | 10.2210/pdb2npq/pdb |
| Descriptor | Mitogen-activated protein kinase 14, octyl beta-D-glucopyranoside (3 entities in total) |
| Functional Keywords | lipid binding site, kinase, protein-lipid complex, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 42827.89 |
| Authors | Diskin, R.,Engelberg, D.,Livnah, O. (deposition date: 2006-10-29, release date: 2007-10-16, Last modification date: 2023-10-25) |
| Primary citation | Diskin, R.,Engelberg, D.,Livnah, O. A novel lipid binding site formed by the MAP kinase insert in p38 alpha. J.Mol.Biol., 375:70-79, 2008 Cited by PubMed Abstract: The p38 mitogen-activated protein (MAP) kinases function as signaling molecules essential for many cellular processes, particularly mediating stress response. The activity of p38 MAP kinases is meticulously regulated to reach the desired cellular phenotype. Several alternative activation and attenuation mechanisms have been characterized recently which include new phosphorylation sites. Here we present the crystal structure of p38 alpha MAP kinase in complex with n-octyl-beta-glucopyranoside detergent. The complex unveils a novel lipid-binding site formed by a local conformational change of the MAP kinase insert. This binding is the first attribution for a possible role of the MAP kinase insert in p38. The binding site can accommodate a large selection of lipidic molecules. In addition, we also show via biophysical methods that arachidonic acid and its derivatives bind p38 alpha in vitro. Based on our analysis we propose that the binding of lipids could fine-tune p38 alpha catalytic activity towards a preferred phenotype. PubMed: 17999933DOI: 10.1016/j.jmb.2007.09.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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