SandboxPKA: Difference between revisions

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[[Image:figura1jc.jpg|thumb|left|'''c-Abl/Bcr-Abl diagram:''' (a): c-Abl gene. The diagram includes N-terminal “cap”, SH3 domain, SH2 domain. It is myristoylated (b)Bcr-Abl fusion protein: is not myristoylated.]]

All of the protein kinases have a similar bilobal fold, and their key structural features have been well studied. Like others, the abelson kinase incorporates a highly conserved bi-lobed structure with an adenosine triphosphate (ATP) binding domain situated in a deep cleft between the N- and C-terminal lobes. Adjacent to this is the centrally located activation loop that incorporates a conserved Asp-Phe-Gly (DFG) sequence and controls catalytic activity by switching between different states in a phosphorylation-dependent manner <ref>PMID:16203792.</ref>.

All of the protein kinases have a similar bilobal fold, and their key structural features have been well studied. Like others, the abelson kinase incorporates a highly conserved bi-lobed structure with an adenosine triphosphate (ATP) binding domain situated in a deep cleft between the N- and C-terminal lobes. Adjacent to this is the centrally located activation loop that incorporates a conserved Asp-Phe-Gly (DFG) sequence and controls catalytic activity by switching between different states in a phosphorylation-dependent manner <ref>PMID:16203792</ref>.

The N-terminal half of the protein includes an N-terminal “cap” of 80 residues that is important for autoinhibition, followed by an SH3 domain, an SH2 domain, and a tyrosine kinase domain. The C-terminal half of c-Abl includes binding elements for SH3 domains, nuclear localization and export signals, a DNA binding functionality, and an actin binding domain. Human cells express two splice variants of c-Abl, Abl 1a and Abl 1b, which differ only in the very N-terminal region. Abl 1b is myristoylated, whereas Abl1a is not.

SandboxPKA: Difference between revisions

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@@ Line 9: / Line 9: @@
 [[Image:figura1jc.jpg|thumb|left|'''c-Abl/Bcr-Abl diagram:''' (a): c-Abl gene. The diagram includes N-terminal “cap”, SH3 domain, SH2 domain. It is myristoylated (b)Bcr-Abl fusion protein: is not myristoylated.]]
-All of the protein kinases have a similar bilobal fold, and their key structural features have been well studied.  Like others, the abelson kinase incorporates a highly conserved bi-lobed structure with an adenosine triphosphate (ATP) binding domain situated in a deep cleft between the N- and C-terminal lobes. Adjacent to this is the centrally located activation loop that incorporates a conserved Asp-Phe-Gly (DFG) sequence and controls catalytic activity by switching between different states in a phosphorylation-dependent manner <ref>PMID:16203792.</ref>.
+All of the protein kinases have a similar bilobal fold, and their key structural features have been well studied.  Like others, the abelson kinase incorporates a highly conserved bi-lobed structure with an adenosine triphosphate (ATP) binding domain situated in a deep cleft between the N- and C-terminal lobes. Adjacent to this is the centrally located activation loop that incorporates a conserved Asp-Phe-Gly (DFG) sequence and controls catalytic activity by switching between different states in a phosphorylation-dependent manner <ref>PMID:16203792</ref>.
 The N-terminal half of the protein includes an N-terminal “cap” of 80 residues that is important for autoinhibition, followed by an SH3 domain, an SH2 domain, and a tyrosine kinase domain. The C-terminal half of c-Abl includes binding elements for SH3 domains, nuclear localization and export signals, a DNA binding functionality, and an actin binding domain. Human cells express two splice variants of c-Abl, Abl 1a and Abl 1b, which differ only in the very N-terminal region. Abl 1b is myristoylated, whereas Abl1a is not.