1u59
From Proteopedia
(New page: 200px<br /> <applet load="1u59" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u59, resolution 2.30Å" /> '''Crystal Structure o...) |
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caption="1u59, resolution 2.30Å" /> | caption="1u59, resolution 2.30Å" /> | ||
'''Crystal Structure of the ZAP-70 Kinase Domain in Complex with Staurosporine'''<br /> | '''Crystal Structure of the ZAP-70 Kinase Domain in Complex with Staurosporine'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1U59 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 STU 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:// | + | 1U59 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=STU:'>STU</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=1U59 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 14:59, 15 February 2008
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Crystal Structure of the ZAP-70 Kinase Domain in Complex with Staurosporine
Contents |
Overview
The ZAP-70 tyrosine kinase plays a critical role in T cell activation and, the immune response and therefore is a logical target for immunomodulatory, therapies. Although the crystal structure of the tandem Src homology-2, domains of human ZAP-70 in complex with a peptide derived from the zeta, subunit of the T cell receptor has been reported (Hatada, M. H., Lu, X., Laird, E. R., Green, J., Morgenstern, J. P., Lou, M., Marr, C. S., Phillips, T. B., Ram, M. K., Theriault, K., Zoller, M. J., and Karas, J., L. (1995) Nature 377, 32-38), the structure of the kinase domain has been, elusive to date. We crystallized and determined the three-dimensional, structure of the catalytic subunit of ZAP-70 as a complex with, staurosporine to 2.3 A resolution, utilizing an active kinase domain, containing residues 327-606 identified by systematic N- and C-terminal, truncations. The crystal structure shows that this ZAP-70 kinase domain is, in an active-like conformation despite the lack of tyrosine, phosphorylation in the activation loop. The unique features of the, ATP-binding site, identified by structural and sequence comparison with, other kinases, will be useful in the design of ZAP-70-selective, inhibitors.
Disease
Known diseases associated with this structure: Selective T-cell defect OMIM:[176947]
About this Structure
1U59 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the ZAP-70 kinase domain in complex with staurosporine: implications for the design of selective inhibitors., Jin L, Pluskey S, Petrella EC, Cantin SM, Gorga JC, Rynkiewicz MJ, Pandey P, Strickler JE, Babine RE, Weaver DT, Seidl KJ, J Biol Chem. 2004 Oct 8;279(41):42818-25. Epub 2004 Jul 29. PMID:15292186
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