From Proteopedia
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| <Structure load='1opl' size='400' frame='true' align='right' caption='ABL1 homo-dimer complex' scene='SandboxPKA/Abl1_homo-dimer_complex/1'' /> | | <Structure load='1opl' size='400' frame='true' align='right' caption='ABL1 homo-dimer complex' scene='SandboxPKA/Abl1_homo-dimer_complex/1'' /> |
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Revision as of 21:46, 4 December 2012
Introduction
The c-Abl protein 1 (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. In more than 90% cases, chronic myelogeneous leukemia (CML) is caused by chromosomal abnormality resulting in the formation of a so-called Philadelphia chromosome. It is caused by (9;22) chromosomal-translocation and results in the head-to-tail fusion of the BCR and ABL1, leading a constitutive activation of this tyrosine kinase.
Structure
kjnkjkj
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Morado dominio SH3
Rojo dominio SH2
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Catalytic domain
It 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:
• ATP-binding pocket: is mainly mediated by alfa-helix
• Protein-binding pocket: lamina-B domain
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