Hello Rachelle,Many thanks for sharing the link and for your kind help. I
could read the abstract only and failed to get the PDF of the full text due to
access issues. Is it possible to kindly send the paper if that is Ok with you?
If there will be any copyright issues, please do not worry about it.Thank you
again. I really appreciate it.Best regards,Samer
On Friday, August 7, 2020, 03:21:05 PM GMT+1, Gaudet, Rachelle
<gau...@mcb.harvard.edu> wrote:
Hi Samer,
Adding to Pascal’s list, calmodulin is another protein with many methionines
that provide a flexible binding site. See this review as a starting point for
reading about it:https://pubmed.ncbi.nlm.nih.gov/9923700/.
Best,
Rachelle
___________________________________________________________________
Rachelle Gaudet, Ph.D.
Professor of Molecular and Cellular Biology
Co-Director of Undergraduate Studies, Chemical and Physical Biology
Harvard University
52 Oxford Street
Cambridge, MA 02138
Voice: (617) 495-5616 e-mail: gau...@mcb.harvard.edu
___________________________________________________________________
From: CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> On Behalf Of Pascal Egea
Sent: Friday, August 7, 2020 10:21 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: Re: [ccp4bb] Structural Importance of Methionine
Hi Samer,
In addition to what has been already mentioned to you, there are also the two
well illustrated cases of methionine rich domains.
- in the case of the M (for Met rich) domain of the Signal Recognition Particle
protein SRP54/Ffh involved in promiscuous binding of the N-terminal hydrophobic
signal sequences of nascent membrane proteins as they exit the ribosome en
route to the translocon and the membrane for insertion or secretion.
- in the case of the ATP-ase Get3 (Guided Entry of Tail anchored proteins) 2
that also has an hydrophobic cleft enriched in Met residues also designed to
promiscuously bind the hydrophobic C-terminal transmembrane helices of
so-called Tailed Anchored proteins.
In both cases the substrates are hydrophobic helices and the greasy and
flexible side chains of Methionines of the receptor protein (SRP54/Ffh or Get3)
can accommodate a variety of hydrophobic substrates in the protein binding
clefts.
I hope this helps you.
All the best,
Pascal
On Fri, Aug 7, 2020 at 5:14 AM samer halabi
<000030c2162795b2-dmarc-requ...@jiscmail.ac.uk> wrote:
Dear All,
I am working on structures where Methionine is important in binding of peptides
to the MHC protein complex.
Would anyone kindly like to share their knowledge about anything they find it
important about this particular amino acid structurally? Sharing a paper or
just few comments will be greatly appreciated.
I know my question may sound very general (and kind of superficial) but there
is definitely a reason, that I don't know and might be already known, why
certain peptides (like CLIP) are rich in Methionine, and that lowers their
affinity of binding.
Thank you and sorry to disturb you all.
Best regards,
Samer
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Pascal F. Egea, PhD
Associate Project Scientist
UCLA, David Geffen School of Medicine
Department of Biological Chemistry
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