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<mailto: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<mailto: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<https://urldefense.proofpoint.com/v2/url?u=https-3A__www.jiscmail.ac.uk_cgi-2Dbin_WA-2DJISC.exe-3FSUBED1-3DCCP4BB-26A-3D1&d=DwMFaQ&c=WO-RGvefibhHBZq3fL85hQ&r=zarhu_AFfXHIr7BLs8GQXPvC2gpkmnikRXKYvnCJnk0&m=FpV2vp6oO-Ox53M7Ncww74udjlwJMJXwqJ_i-3DFZv4&s=gmuTxUEHrZ6ZtiOB-dDVGLUQs1EgipJhjkBC0O24LHQ&e=> -- 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<https://urldefense.proofpoint.com/v2/url?u=http-3A__mednet.ucla.edu&d=DwMFaQ&c=WO-RGvefibhHBZq3fL85hQ&r=zarhu_AFfXHIr7BLs8GQXPvC2gpkmnikRXKYvnCJnk0&m=FpV2vp6oO-Ox53M7Ncww74udjlwJMJXwqJ_i-3DFZv4&s=fFkbpZheDOEaefToqqTQ-h4wEjpuzPAc8QJzA7SJDn8&e=> ________________________________ To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1<https://urldefense.proofpoint.com/v2/url?u=https-3A__www.jiscmail.ac.uk_cgi-2Dbin_WA-2DJISC.exe-3FSUBED1-3DCCP4BB-26A-3D1&d=DwMFaQ&c=WO-RGvefibhHBZq3fL85hQ&r=zarhu_AFfXHIr7BLs8GQXPvC2gpkmnikRXKYvnCJnk0&m=FpV2vp6oO-Ox53M7Ncww74udjlwJMJXwqJ_i-3DFZv4&s=gmuTxUEHrZ6ZtiOB-dDVGLUQs1EgipJhjkBC0O24LHQ&e=> ######################################################################## 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/
