1mqb: Difference between revisions

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[[Image:1mqb.gif|left|200px]]<br /><applet load="1mqb" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1mqb.gif|left|200px]]
caption="1mqb, resolution 2.30&Aring;" />
 
'''Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase'''<br />
{{Structure
|PDB= 1mqb |SIZE=350|CAPTION= <scene name='initialview01'>1mqb</scene>, resolution 2.30&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2]
|GENE= EphA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1MQB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQB OCA].  
1MQB 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=1MQB OCA].  


==Reference==
==Reference==
Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography., Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA, Structure. 2002 Dec;10(12):1659-67. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12467573 12467573]
Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography., Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA, Structure. 2002 Dec;10(12):1659-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12467573 12467573]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: tyrosine protein kinase]]
[[Category: tyrosine protein kinase]]


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Revision as of 13:46, 20 March 2008

File:1mqb.gif


PDB ID 1mqb

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands:
Gene: EphA2 (Homo sapiens)
Activity: Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase


OverviewOverview

Protein kinases are important drug targets in human cancers, inflammation, and metabolic diseases. This report presents the structures of kinase domains for three cancer-associated protein kinases: ephrin receptor A2 (EphA2), focal adhesion kinase (FAK), and Aurora-A. The expression profiles of EphA2, FAK, and Aurora-A in carcinomas suggest that inhibitors of these kinases may have inherent potential as therapeutic agents. The structures were determined from crystals grown in nanovolume droplets, which produced high-resolution diffraction data at 1.7, 1.9, and 2.3 A for FAK, Aurora-A, and EphA2, respectively. The FAK and Aurora-A structures are the first determined within two unique subfamilies of human kinases, and all three structures provide new insights into kinase regulation and the design of selective inhibitors.

About this StructureAbout this Structure

1MQB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography., Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA, Structure. 2002 Dec;10(12):1659-67. PMID:12467573

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