I have a test tomorrow and while I was going through a practice problem I encounted a problem. The section that covers this problem was lectured on by a TA and he wasnt very clear on this part. The problem says:
What distinguishing features of serine, threonine, and tyrosine make them the amino acids of choice for kinases?
I know its the alcohol group, but not 100% sure why. Im thinking that it facilitates phosphorylation, but not really sure on that.
What determines whether a particular serine/threonin/tyrosine is modified by a particular kinase?
Im pretty sure this is the particular motif of amino acid side chains surrounding the particular serine/threonine/tyrosine allows the kinase to "target" the serine and others for phosphorylation. But what Im confused on was I thought that the with serine/threonine and tyrosine receptor kinases were unique in that the tyrosine residues (for example) phosphorylate eachother when the receptors dimerize (autophosphorylation). If this is true (which it is) then what role does the kinase play in phosphorylation?
^^^^ my main question
What distinguishing features of serine, threonine, and tyrosine make them the amino acids of choice for kinases?
I know its the alcohol group, but not 100% sure why. Im thinking that it facilitates phosphorylation, but not really sure on that.
What determines whether a particular serine/threonin/tyrosine is modified by a particular kinase?
Im pretty sure this is the particular motif of amino acid side chains surrounding the particular serine/threonine/tyrosine allows the kinase to "target" the serine and others for phosphorylation. But what Im confused on was I thought that the with serine/threonine and tyrosine receptor kinases were unique in that the tyrosine residues (for example) phosphorylate eachother when the receptors dimerize (autophosphorylation). If this is true (which it is) then what role does the kinase play in phosphorylation?
^^^^ my main question

. Thanks again.