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1、The Biophysical Society of Japan General Incorporated Association NII-Electronic Library Service TheBiophysical Society of Japan General IncorporatedAssociation SIM-1 NMR studies of periplasmic binding proteins CYLitttku Ttei2, Kaori Kurashimu-Ito?, Kayane Moromisatoi, Takao Inoue. Kaoru Nishirnura3
2、, Jonathan Heddlei, Jereiny TameS, Masaki Mishimai iDepartment of Chetnistry, Tokyo Metropolitan University, 2Researeh Croup for Bie-macromolecular Structure-Function, RIKEN, SProtein Dcsign I.aboralory, Ylkohama City Universiy Recent deveropments on prorein stable isotope labeling and TTOSYtbased N
3、MR mcasuremenrs were applied to a 56kDa (502 a,a,) Escherichia eoli NikA ancl a 59kDa (517 a.a.) Salmonela typhimuriuni OppA.NikA is the periplasmic nickcl- binding protein requiied for nickel transpott Lnd chenetactic response by E, coli. Assignments fT m(iTc Lhan 86% ef non-preline Tesidues were e
4、btaiiied by the allalysis of TROSYLbased triple-rcsenancc experiments. For around 10ff of non- proline rcsiducs, IH-ISN corrclation cross pcaks wcrc not detected in IH-15N TROSYLHSQC spectru. These unobservableii residues were found lo be located around the Ni-binding pecket, identified by mapping L
5、he residLLes onto the recenty determined vrsta1 stnictures of apo- and Ni-bound NikiX. This rcsulL suggested a oeal eonfbrmational fiexibility around the Ni-binding pockct iti Ni-frce state. OppA has a rcmarkably bread substratc specifieity. binding peptides ef two or five amino-acid residues with h
6、igh affinity, but iule regard to sequence. It is thereforc an idcaL systcm for studying how diitcrent chemical groups can be accuinmedated in a protein interior, By applying a similar TROSYLbased NMR approach, nlorc than 9% nf non-proline residues have been assigned. As in the case of NikA, the 10%
7、iunohservublei residues were located areund thc ligand-binding pocket, suggesling u uommon ligund-recognnion mechanism of periptasniic bindin.g. protelns, SIM-2 High field NrYIR studies for the structure and interaction of disease-relatedproteins OChuejoon Cheo.ui, Hae Kap Cheong, Keung-Seok R)ui, S
8、eung-Cheol Leei. Kwan Soo HongG, Young-He Jeon2 iDiv, ot Slruclural Protcumics, Korca Basic Science institute. 2Magnetic Resonanee Teatn. Korea Basic Scjcncc Institutc, Magnetic Rcsonancc Imaging Tcam, Korca Basic Science Institute Due to the discoveny vf functional genomics and preteomiLh many prot
9、eins rclatc(l with discasc precess arc idcntilicd wilh trcmendously high specd, Thcse diseasc-rclated protcjns arc now chamging rhc way of drug discovcry and thc ncw teehnelogies speed up the discovery process. Rational dru.g. designs based on protein structures aTe emerging as a promising technoleg
10、y ft)r fasteT drug diseeveTy because they catl help researchets design drug leads efficiently. NMR can provide valuable information for thc srmcturc-based drug diseovcLlr, including 3D structures of active sites, protein-ligand interactions. and possiblc conformational chunges upon billdimg of ligai
11、ids. Here we preseiit some examples of NMR bused suuetural studies for disease-related proteins. The results include 3D stntctural features of biotinyl carboxyl carrier protein (BCCP) domain of Acety1-coenzyme A carboxylasc (ACC), a ubiquitin-likc protein, and DNA rcplicatien licensing rclated prete
12、in. va- also repert oLtr new resLtts ef MR micioimagiig und rm uiiimal imaging, With an advanecmcnt uf magnetic rcsoaiice Lechnolegy, we cuuld follo- develepmcntal cvcnts froin as early as the firsT cleavagc stage to thc early tailbud stage sequcntially. Temporal emid spatial resolutions have been i
13、nrpres:ed. mid eonsequently suhcellular dynamie events inside an ernbryo during developrnent could be reveuled. SIM-3 In vitro and in cell NMR studies uf modifier proteins OMasahiro Shiraka;vai:. Tomomi Sakai. Hidchito Tochiuij, Tetsuro Kekubo3A. Sewon Ki4, Fuminori SugihaTa. Daichi Bzha , Hideka7u
14、Hiroaki GTaduute Schoo1 of Engineering, Kyote Uniyersity 2RIKEN Genomic Seience Center, CREST, Japan Science and Technology Corporation 4Systems GTaduate School of Integrated Science, Yokoharna City Uni s,ersity Modifieationsofintraceljuarproteinsbyubiquitinrits-reiatedmodlfierproteins, such as SUMO
15、, exerts signaling fullctiens that mediate a vvide raiige of cellular processes.Chains oT sngle molecuies ef llbiguitin can be att-=hed te preteins, Of yarious femis ef polyubiquiim chaiiis so ftir reported, bys 48- and Lys 6-linked pelynbiqnitin have heen functlonally well charaeterized, which are
16、involved in distinet functions. Attachment of .ys 48-linked chain generally target moddicd proteins for degTadation by the proteasome, whie Lys 63-linked chaii js involvcd in various ceilutar events, such as DNA repuir. activatLon of lkB kinase and ribosome functioll. not relying on degradative signaling via the proteasorne. k churacterize their eenfbmiations, we analyzed illtersubunit interfaces ef bys 63- and Lys 48-1inked di- and tetraubiquitin chains by isotop
