User:Alice Harmon/Sandbox 1: Difference between revisions

Line 66:

===Regulation of Protein Kinase Activity===

There are a variety of ways that the activity of protein kinases are regulated. Here are a few examples. Some are regulated via phosphorylation of residue(s) in the activation loop by either an upstream protein kinase (such as [[mitogen-activated protein kinase]] phosphorylation by MAPKK) or by autophosphosphorylation stimulated by the binding of a ligand (such as the insulin receptor kinase<ref>PMID:7997262</ref>). Others are activated by binding with other proteins, which brings the kinase into the active conformation. The PKA C subunit, having been constitutively phosphorylated by an upstream kinase, is active when released from a complex with the regulatory subunit upon the binding of cAMP (see [[~~http://proteopedia.org/wiki/index.php/CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit~~]]. Calcium-dependent protein kinase has calcium-binding domain that blocks the active site in the absence of calcium<ref>PMID:20436473</ref>. Upon binding calcium the latter domain undergoes a dramatic conformational change and it moves to a binding site that is on opposite side of the kinase, thus unblocking the catalytic cleft.

There are a variety of ways that the activity of protein kinases are regulated. Here are a few examples. Some are regulated via phosphorylation of residue(s) in the activation loop by either an upstream protein kinase (such as [[mitogen-activated protein kinase]] phosphorylation by MAPKK) or by autophosphosphorylation stimulated by the binding of a ligand (such as the insulin receptor kinase<ref>PMID:7997262</ref>). Others are activated by binding with other proteins, which brings the kinase into the active conformation. The PKA C subunit, having been constitutively phosphorylated by an upstream kinase, is active when released from a complex with the regulatory subunit upon the binding of cAMP (see [[cAMP-dependent protein kinase]]). Calcium-dependent protein kinase has calcium-binding domain that blocks the active site in the absence of calcium<ref>PMID:20436473</ref>. Upon binding calcium the latter domain undergoes a dramatic conformational change and it moves to a binding site that is on opposite side of the kinase, thus unblocking the catalytic cleft.

=References=

@@ Line 66: / Line 66: @@
 ===Regulation of Protein Kinase Activity===
-There are a variety of ways that the activity of protein kinases are regulated. Here are a few examples. Some are regulated via phosphorylation of residue(s) in the activation loop by either an upstream protein kinase (such as [[mitogen-activated protein kinase]] phosphorylation by MAPKK) or by autophosphosphorylation stimulated by the binding of a ligand (such as the insulin receptor kinase<ref>PMID:7997262</ref>). Others are activated by binding with other proteins, which brings the kinase into the active conformation. The PKA C subunit, having been constitutively phosphorylated by an upstream kinase, is active when released from a complex with the regulatory subunit upon the binding of cAMP (see [[http://proteopedia.org/wiki/index.php/CAMP_Dependent_Protein_Kinase%2C_Catalytic_Subunit]]. Calcium-dependent protein kinase has calcium-binding domain that blocks the active site in the absence of calcium<ref>PMID:20436473</ref>. Upon binding calcium the latter domain undergoes a dramatic conformational change and it moves to a binding site that is on opposite side of the kinase, thus unblocking the catalytic cleft.
+There are a variety of ways that the activity of protein kinases are regulated. Here are a few examples. Some are regulated via phosphorylation of residue(s) in the activation loop by either an upstream protein kinase (such as [[mitogen-activated protein kinase]] phosphorylation by MAPKK) or by autophosphosphorylation stimulated by the binding of a ligand (such as the insulin receptor kinase<ref>PMID:7997262</ref>). Others are activated by binding with other proteins, which brings the kinase into the active conformation. The PKA C subunit, having been constitutively phosphorylated by an upstream kinase, is active when released from a complex with the regulatory subunit upon the binding of cAMP (see [[cAMP-dependent protein kinase]]). Calcium-dependent protein kinase has calcium-binding domain that blocks the active site in the absence of calcium<ref>PMID:20436473</ref>. Upon binding calcium the latter domain undergoes a dramatic conformational change and it moves to a binding site that is on opposite side of the kinase, thus unblocking the catalytic cleft.
 =References=
 <references/>