1wfc: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1wfc.jpg|left|200px]] | [[Image:1wfc.jpg|left|200px]] | ||
'''STRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN ACTIVATED PROTEIN KINASE P38 (P38 MAP KINASE) THE MAMMALIAN HOMOLOGUE OF THE YEAST HOG1 PROTEIN''' | {{Structure | ||
|PDB= 1wfc |SIZE=350|CAPTION= <scene name='initialview01'>1wfc</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN ACTIVATED PROTEIN KINASE P38 (P38 MAP KINASE) THE MAMMALIAN HOMOLOGUE OF THE YEAST HOG1 PROTEIN''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1WFC is a [ | 1WFC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WFC OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of p38 mitogen-activated protein kinase., Wilson KP, Fitzgibbon MJ, Caron PR, Griffith JP, Chen W, McCaffrey PG, Chambers SP, Su MS, J Biol Chem. 1996 Nov 1;271(44):27696-700. PMID:[http:// | Crystal structure of p38 mitogen-activated protein kinase., Wilson KP, Fitzgibbon MJ, Caron PR, Griffith JP, Chen W, McCaffrey PG, Chambers SP, Su MS, J Biol Chem. 1996 Nov 1;271(44):27696-700. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8910361 8910361] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:56:15 2008'' | ||
Revision as of 15:56, 20 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN ACTIVATED PROTEIN KINASE P38 (P38 MAP KINASE) THE MAMMALIAN HOMOLOGUE OF THE YEAST HOG1 PROTEIN
OverviewOverview
p38 mitogen-activated protein kinase is activated by environmental stress and cytokines and plays a role in transcriptional regulation and inflammatory responses. The crystal structure of the apo, unphosphorylated form of p38 kinase has been solved at 2.3 A resolution. The fold and topology of p38 is similar to ERK2 (Zhang, F., Strand, A., Robbins, D., Cobb, M. H., and Goldsmith, E. J. (1994) Nature 367, 704-711). The relative orientation of the two domains of p38 kinase is different from that observed in the active form of cAMP-dependent protein kinase. The twist results in a misalignment of the active site of p38, suggesting that the orientation of the domains would have to change before catalysis could proceed. The residues that are phosphorylated upon activation of p38 are located on a surface loop that occupies the peptide binding channel. Occlusion of the active site by the loop, and misalignment of catalytic residues, may account for the low enzymatic activity of unphosphorylated p38 kinase.
About this StructureAbout this Structure
1WFC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of p38 mitogen-activated protein kinase., Wilson KP, Fitzgibbon MJ, Caron PR, Griffith JP, Chen W, McCaffrey PG, Chambers SP, Su MS, J Biol Chem. 1996 Nov 1;271(44):27696-700. PMID:8910361
Page seeded by OCA on Thu Mar 20 14:56:15 2008