SandboxPKA
From Proteopedia
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<StructureSection load='1OPK' size='350' side='right' caption='c-Abl tyrosine kinase' scene='SandboxPKA/Abl1/4'> | <StructureSection load='1OPK' size='350' side='right' caption='c-Abl tyrosine kinase' scene='SandboxPKA/Abl1/4'> | ||
- | Anything in this section will appear adjacent to the 3D structure and will be scrollable. | ||
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Morado dominio SH3 | Morado dominio SH3 | ||
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== '''Catalytic domain''' == | == '''Catalytic domain''' == | ||
+ | is responsible of both, ATP binding as well as protein binding. | ||
- | < | + | <StructureSection load='3DY7' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> |
Catalitic subunit of c-Abl protein is composed by two different regions: | Catalitic subunit of c-Abl protein is composed by two different regions: |
Revision as of 17:28, 4 December 2012
ABL1, also known as Abelson kinase, is a non-receptor tyrosine kinase that plays a role in many key processes linked to cell growth and survival. Activity of c-Abl protein is negatively regulated by its SH3 domain, and deletion of the SH3 domain turns ABL1 into an oncogene. The t(9;22) translocation results in the head-to-tail fusion of the BCR and ABL1 genes present in many cases of chronic myelogeneous leukemia.
Structure
Abl-BCR es .....
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Catalytic domain
is responsible of both, ATP binding as well as protein binding.
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Catalitic subunit of c-Abl protein is composed by two different regions:
Dentro del core de la akt, tenemos dos regiones: • ATP-binding pocket: is mainly mediated by alfa-helix • Protein-binding pocket: lamina-B domain