1ksw: Difference between revisions
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|PDB= 1ksw |SIZE=350|CAPTION= <scene name='initialview01'>1ksw</scene>, resolution 2.8Å | |PDB= 1ksw |SIZE=350|CAPTION= <scene name='initialview01'>1ksw</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NBS:N6-BENZYL ADENOSINE-5'-DIPHOSPHATE'>NBS</scene> | |LIGAND= <scene name='pdbligand=NBS:N6-BENZYL+ADENOSINE-5'-DIPHOSPHATE'>NBS</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1fmk|1FMK]], [[2src|2SRC]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ksw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksw OCA], [http://www.ebi.ac.uk/pdbsum/1ksw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ksw RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
The direct substrates of one protein kinase in a cell can be identified by mutation of the ATP binding pocket to allow an unnatural ATP analog to be accepted exclusively by the engineered kinase. Here, we present structural and functional assessment of peptide specificity of mutant protein kinases with unnatural ATP analogs. The crystal structure (2.8 A resolution) of c-Src (T338G) with N(6)-(benzyl) ADP bound shows that the creation of a unique nucleotide binding pocket does not alter the phospho-acceptor binding site of the kinase. A panel of optimal peptide substrates of defined sequence, as well as a degenerate peptide library, was utilized to assess the phospho-acceptor specificity of the engineered "traceable" kinases. The specificity profiles for the mutant kinases were found to be identical to those of their wild-type counterparts. | The direct substrates of one protein kinase in a cell can be identified by mutation of the ATP binding pocket to allow an unnatural ATP analog to be accepted exclusively by the engineered kinase. Here, we present structural and functional assessment of peptide specificity of mutant protein kinases with unnatural ATP analogs. The crystal structure (2.8 A resolution) of c-Src (T338G) with N(6)-(benzyl) ADP bound shows that the creation of a unique nucleotide binding pocket does not alter the phospho-acceptor binding site of the kinase. A panel of optimal peptide substrates of defined sequence, as well as a degenerate peptide library, was utilized to assess the phospho-acceptor specificity of the engineered "traceable" kinases. The specificity profiles for the mutant kinases were found to be identical to those of their wild-type counterparts. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Shokat, K M.]] | [[Category: Shokat, K M.]] | ||
[[Category: Witucki, L A.]] | [[Category: Witucki, L A.]] | ||
[[Category: atp]] | [[Category: atp]] | ||
[[Category: bump hole]] | [[Category: bump hole]] | ||
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[[Category: sh3]] | [[Category: sh3]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:53:07 2008'' | ||
