2jbp: Difference between revisions

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[[Image:2jbp.jpg|left|200px]]
{{Seed}}
[[Image:2jbp.png|left|200px]]


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{{STRUCTURE_2jbp|  PDB=2jbp  |  SCENE=  }}  
{{STRUCTURE_2jbp|  PDB=2jbp  |  SCENE=  }}  


'''PROTEIN KINASE MK2 IN COMPLEX WITH AN INHIBITOR (CRYSTAL FORM-2, CO-CRYSTALLIZATION)'''
===PROTEIN KINASE MK2 IN COMPLEX WITH AN INHIBITOR (CRYSTAL FORM-2, CO-CRYSTALLIZATION)===




==Overview==
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The Ser/Thr protein kinase MAPKAP kinase 2 (MK2) plays a crucial role in inflammation. We determined the structure of the kinase domain of MK2 in complex with a low molecular mass inhibitor in two different crystal forms, obtained from soaking and co-crystallization. To our knowledge, these are the first structures of MK2 showing the binding mode of an inhibitor with high binding affinity (IC50 8.5 nM). The two crystal forms revealed conformational flexibility in the binding site and extend the experimental basis for rational drug design. Crystal form-1 contained one MK2 molecule per asymmetric unit. Form-2 contained 12 molecules, which arrange into two different types of MK2 trimers. One of them may serve as a model for an intermediate state during substrate phosphorylation, as each MK2 monomer places its activation segment into the substrate peptide binding groove of the trimer neighbor.
The line below this paragraph, {{ABSTRACT_PUBMED_17449059}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_17449059}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural basis for a high affinity inhibitor bound to protein kinase MK2., Hillig RC, Eberspaecher U, Monteclaro F, Huber M, Nguyen D, Mengel A, Muller-Tiemann B, Egner U, J Mol Biol. 2007 Jun 8;369(3):735-45. Epub 2007 Mar 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17449059 17449059]
Structural basis for a high affinity inhibitor bound to protein kinase MK2., Hillig RC, Eberspaecher U, Monteclaro F, Huber M, Nguyen D, Mengel A, Muller-Tiemann B, Egner U, J Mol Biol. 2007 Jun 8;369(3):735-45. Epub 2007 Mar 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17449059 17449059]
Identifying protein construct variants with increased crystallization propensity--a case study., Malawski GA, Hillig RC, Monteclaro F, Eberspaecher U, Schmitz AA, Crusius K, Huber M, Egner U, Donner P, Muller-Tiemann B, Protein Sci. 2006 Dec;15(12):2718-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17132859 17132859]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Small molecule inhibitor]]
[[Category: Small molecule inhibitor]]
[[Category: Transferase]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:39:27 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:45:46 2008''

Revision as of 10:45, 29 July 2008

File:2jbp.png

Template:STRUCTURE 2jbp

PROTEIN KINASE MK2 IN COMPLEX WITH AN INHIBITOR (CRYSTAL FORM-2, CO-CRYSTALLIZATION)

Template:ABSTRACT PUBMED 17449059

About this Structure

2JBP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for a high affinity inhibitor bound to protein kinase MK2., Hillig RC, Eberspaecher U, Monteclaro F, Huber M, Nguyen D, Mengel A, Muller-Tiemann B, Egner U, J Mol Biol. 2007 Jun 8;369(3):735-45. Epub 2007 Mar 12. PMID:17449059

Identifying protein construct variants with increased crystallization propensity--a case study., Malawski GA, Hillig RC, Monteclaro F, Eberspaecher U, Schmitz AA, Crusius K, Huber M, Egner U, Donner P, Muller-Tiemann B, Protein Sci. 2006 Dec;15(12):2718-28. PMID:17132859

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