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 > > ------------------------------ > > To unsubscribe from the CCP4BB list, click the following link: > https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 > -- Pascal F. Egea, PhD Associate Project Scientist UCLA, David Geffen School of Medicine Department of Biological Chemistry Boyer Hall room 356 611 Charles E Young Drive East Los Angeles CA 90095 office (310)-983-3515 lab (310)-983-3516 email pegea at mednet.ucla.edu ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
