3lck
From Proteopedia
(New page: 200px<br /> <applet load="3lck" size="450" color="white" frame="true" align="right" spinBox="true" caption="3lck, resolution 1.70Å" /> '''THE KINASE DOMAIN O...) |
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caption="3lck, resolution 1.70Å" /> | caption="3lck, resolution 1.70Å" /> | ||
'''THE KINASE DOMAIN OF HUMAN LYMPHOCYTE KINASE (LCK), ACTIVATED FORM (AUTO-PHOSPHORYLATED ON TYR394)'''<br /> | '''THE KINASE DOMAIN OF HUMAN LYMPHOCYTE KINASE (LCK), ACTIVATED FORM (AUTO-PHOSPHORYLATED ON TYR394)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3LCK 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 SO4 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:// | + | 3LCK 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=SO4:'>SO4</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=3LCK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tyrosine-protein kinase]] | [[Category: tyrosine-protein kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:43:46 2008'' |
Revision as of 15:43, 15 February 2008
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THE KINASE DOMAIN OF HUMAN LYMPHOCYTE KINASE (LCK), ACTIVATED FORM (AUTO-PHOSPHORYLATED ON TYR394)
Contents |
Overview
Regulation through phosphorylation is a characteristic of signalling, pathways and the lymphocyte kinase Lck (p56lck) both performs, phosphorylation and is affected by it. Lck is a Src-family tyrosine kinase, expressed in T lymphocytes, where it participates in the cellular immune, response. Like all Src homologues, it comprises SH3, SH2 and kinase, domains. Lck associates through its distinctive amino-terminal segment, with the cytoplasmic tails of either T-cell co-receptor, CD4 or CD8-alpha., Activated Lck phosphorylates T-cell receptor zeta-chains, which then, recruit the ZAP70 kinase to promote T-cell activation. Lck is activated by, autophosphorylation at Tyr 394 in the activation loop and it is inactive, when Tyr 505 near the carboxy terminus is phosphorylated and interacts, with its own SH2 domain. Here we report the crystal structure of the Lck, tyrosine kinase domain (LCKK) in its activated state at 1.7 A resolution., The structure reveals how a phosphoryl group at Tyr 394 generates a, competent active site. Comparisons with other kinase structures indicate, that tyrosine phophophorylation and ligand binding may in general elicit, two distinct hinge-like movements between the kinase subdomains. From, modelling studies, we suggest a basis for inhibition by phosphorylation at, Tyr 505.
Disease
Known disease associated with this structure: SCID due to LCK deficiency OMIM:[153390]
About this Structure
3LCK 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
Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation., Yamaguchi H, Hendrickson WA, Nature. 1996 Dec 5;384(6608):484-9. PMID:8945479
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