2cjm

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[[Image:2cjm.gif|left|200px]]<br /><applet load="2cjm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cjm.gif|left|200px]]
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caption="2cjm, resolution 2.30&Aring;" />
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'''MECHANISM OF CDK INHIBITION BY ACTIVE SITE PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX WITH CYCLIN A STRUCTURE'''<br />
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{{Structure
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|PDB= 2cjm |SIZE=350|CAPTION= <scene name='initialview01'>2cjm</scene>, resolution 2.30&Aring;
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37]
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|GENE=
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}}
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'''MECHANISM OF CDK INHIBITION BY ACTIVE SITE PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX WITH CYCLIN A STRUCTURE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2CJM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PTR:'>PTR</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37] Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJM OCA].
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2CJM is a [[Protein complex]] structure of sequences 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=2CJM OCA].
==Reference==
==Reference==
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How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A., Welburn JP, Tucker JA, Johnson T, Lindert L, Morgan M, Willis A, Noble ME, Endicott JA, J Biol Chem. 2007 Feb 2;282(5):3173-81. Epub 2006 Nov 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17095507 17095507]
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How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A., Welburn JP, Tucker JA, Johnson T, Lindert L, Morgan M, Willis A, Noble ME, Endicott JA, J Biol Chem. 2007 Feb 2;282(5):3173-81. Epub 2006 Nov 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17095507 17095507]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:15 2008''

Revision as of 14:16, 20 March 2008

Image:2cjm.gif


PDB ID 2cjm

Drag the structure with the mouse to rotate
, resolution 2.30Å
Sites:
Ligands: , and
Activity: Transferred entry: 2.7.11.1, with EC number 2.7.1.37
Coordinates: save as pdb, mmCIF, xml



MECHANISM OF CDK INHIBITION BY ACTIVE SITE PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX WITH CYCLIN A STRUCTURE


Overview

Inhibition of cyclin-dependent kinase 1 (CDK1) activity by Tyr-15 phosphorylation directly regulates entry into mitosis and is an important element in the control of the unperturbed cell cycle. Active site phosphorylation of other members of the CDK family that regulate cell cycle progression instates checkpoints that are fundamental to eukaryotic cell cycle regulation. Kinetic and crystallographic analyses of CDK2-cyclin A complexes reveal that this inhibitory mechanism operates through steric blockade of peptide substrate binding and through the creation of an environment that favors a non-productive conformation of the terminal group of ATP. By contrast, tyrosine phosphorylation of CDK2 alters neither its Km for ATP nor its significant intrinsic ATPase activity. Tyr-15-phosphorylated CDK2 retains trace protein phosphorylation activity that should be considered in quantitative and qualitative cell cycle models.

About this Structure

2CJM is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A., Welburn JP, Tucker JA, Johnson T, Lindert L, Morgan M, Willis A, Noble ME, Endicott JA, J Biol Chem. 2007 Feb 2;282(5):3173-81. Epub 2006 Nov 9. PMID:17095507

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