Hi Samer, I solved a pair of structures in which a methionine rich amphipathic peptide extending from a coiled coil protein formed two different, fairly intimate crystal contacts in two different crystal forms (see Figure 3). It seems the methionine rich side of this peptide really wanted to be buried against another hydrophobic surface and it wasn't too picky about the nature of the other surface.
https://jvi.asm.org/content/91/2/e01085-16 Best of luck! -Jesscia On Fri, Aug 7, 2020 at 7:40 AM samer halabi < 000030c2162795b2-dmarc-requ...@jiscmail.ac.uk> wrote: > 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 > > > ------------------------------ > > 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 > > ------------------------------ > > To unsubscribe from the CCP4BB list, click the following link: > https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 > -- Jessica Bruhn, Ph.D Principal Scientist NanoImaging Services, Inc. 4940 Carroll Canyon Road, Suite 115 San Diego, CA 92121 Phone #: (888) 675-8261 www.nanoimagingservices.com ######################################################################## 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/
