Dear Mike
yes there are a number of examples of two adjacent residues being
phosphorylated. I remember bovine beta casein for istance. In the old days
of FAB mass spectrometry we defined the phosphorylation sites in the
homologous protein from buffalo. Here is the reference:
P. Petrilli, P. Pucci, H. R. Morris and F. Addeo.
Assignment of phosphorylation sites in buffalo b-casein by Fast Atom
Bombardment mass spectrometry.
Biochem. Biophys. Res. Commun. 140 (1986) 28-37.
Hope this help.
Regards
Piero Pucci
At 16.23 11/06/01 -0400, you wrote:
>Hello.
>
>I am currently working on a phosphorylation project and have a question
>concerning neighboring phosphorylation sites. Does anyone know of an
example of
>two phosphorylateable residues being directly next to each other and both
being
>phosphorylated? Or sites that are very close?
>
>For example:
>
>Directly next to each other:
>
>i.e XXSTXX giving XXSpTpXX upon phosphorylation
>
>Or very close by:
>
>i.e. XXS(X1-2)TXX giving XXSp(X1-2)TpXX upon phosphorylation
>
>I am wondering if phosphorylation of one would sterically hinder the
>phosphorylation of the other. Any instance of these cases that you know
about or
>any insight you have on this issue would be greatly appreciated.
>
>Thanks in advance.
>
>Mike
>
>Mike Curtis
>UMU
>curtism@mail.upstate.edu
>
>
>
Prof. Piero Pucci
Dipartimento di Chimica Organica e Biochimica
Complesso Universitario Monte S. Angelo
via Cinthia - 80134 Napoli
Tel.: 081-674318 - Fax: 081-674313
e
Centro Internazionale Servizi di Spettrometria di Massa
via Pansini 5 - 80131 Napoli
Tel.: 081-5465136 - Fax: 081-5465484
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