1wfc: Difference between revisions

Revision as of 13:31, 28 July 2008

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File:1wfc.png

Template:STRUCTURE 1wfc

STRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN ACTIVATED PROTEIN KINASE P38 (P38 MAP KINASE) THE MAMMALIAN HOMOLOGUE OF THE YEAST HOG1 PROTEINSTRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN ACTIVATED PROTEIN KINASE P38 (P38 MAP KINASE) THE MAMMALIAN HOMOLOGUE OF THE YEAST HOG1 PROTEIN

Template:ABSTRACT PUBMED 8910361

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

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 {{STRUCTURE_1wfc|  PDB=1wfc  |  SCENE=  }}
-'''STRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN ACTIVATED PROTEIN KINASE P38 (P38 MAP KINASE) THE MAMMALIAN HOMOLOGUE OF THE YEAST HOG1 PROTEIN'''
+===STRUCTURE OF APO, UNPHOSPHORYLATED, P38 MITOGEN ACTIVATED PROTEIN KINASE P38 (P38 MAP KINASE) THE MAMMALIAN HOMOLOGUE OF THE YEAST HOG1 PROTEIN===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8910361}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8910361 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8910361}}
 ==About this Structure==
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 [[Category: Serine/threonine protein kinase]]
 [[Category: Transferase]]
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