Structural study of protein p12 from Mason-Pfizer monkey virus using NMR spectroscopy
Project goals
During the maturation of Mason-Pfizer monkey virus polyprotein Gag precursor is cleaved by protease yielding six proteins: p10 (matrix protein - MA), pp24/18, p12, p27 (capsid protein - CA), p14 (nucleocapsid protein - NC) and p4. The functions of pp24/18, p12 and p4 proteins have not been sufficiently explained yet. The deletion mutation experiments in gene encoding protein p12 proved the hypothesis, that this protein supports the assembly of immature viral capsid. The aim of this project is to solve three-dimensional structure of N-terminal domain of protein p12, that could be utilized for a design of suitable inhibitor or viral capsid assembly. The protein will be expressed in E. coli BL21(DE3). Multidimensional NMR spectroscopy on isotopically labeled (15N or 15N,13C) samples together with computational methods will be employed for the solution of three-dimensional structure of this protein.
Keywords
Public support
Provider
Czech Science Foundation
Programme
Post-graduate (doctorate) grants
Call for proposals
Postdoktorandské granty 2 (SGA02002GA-PD)
Main participants
Vysoká škola chemicko-technologická v Praze / Fakulta potravinářské a biochemické technologie
Contest type
VS - Public tender
Contract ID
—
Alternative language
Project name in Czech
Strukturnˇ studie proteinu p12 Mason-Pfizerova opiźˇho viru pomocˇ NMR spektroskopie
Annotation in Czech
Polyproteinově prekurzor Gag Mason-Pfizerova opiźˇho viru je bŘhem maturace rozçtŘpen proteasou na çest protein?: p10 (matrixově protein - MA), pp24/18, p12, p27 (kapsidově protein - CA), p14 (nukleokapsidově protein - NC) a p4. Funkce protein? pp24/18,p12 a p4 dosud nebyla uspokojivŘ vysvŘtlena. Metodou deleźnˇch mutagenezˇ v genu k˘dujˇcˇm protein p12 bylo prok z no, §e tento protein napom h skl d nˇ nezral? virov? kapsidy. Cˇlem tohoto projektu je vyýeçit trojdimenzion lnˇ strukturu N-termin lnˇ dom?ny proteinu p12, na jejˇm§ z kladŘ bude mo§n? navrhnout vhodně inhibitor skl d nˇ virov? kapsidy. Pro pýˇpravu proteinu bude pou§ita metoda exprese v E.coli BL21(DE3). K ýeçenˇ prostorov? struktury proteinu p12 bude vyu§ita vˇcedimenzion lnˇ NMR spektroskopie izotopovŘ obohaceněch (15N nebo 15N, 13C) vzork? spolu s věpoźetnˇmi metodami.
Scientific branches
Completed project evaluation
Provider evaluation
N - Nesplněno zadání
Project results evaluation
Odborně pýˇnos projektu lze spatýovat v objasnŘnˇ pýˇźin tvorby uspoý dan? struktury proteinu P12. édaje ýeçitele jsou zcela adekv tnˇ. Věznam projektu nem pýˇmou aplikaci, pova§uji jej vçak za pýˇnos k pozn nˇ věznamu vyççˇch bˇlkovinněch struktur. Věs
Solution timeline
Realization period - beginning
Jan 1, 2002
Realization period - end
Jan 1, 2004
Project status
S - Stopped (prematurely terminated) multi-year project
Latest support payment
—
Data delivery to CEP
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data delivery code
CEP/2003/GA0/GA03GP/U/N/7:4
Data delivery date
Jun 15, 2009
Finance
Total approved costs
359 thou. CZK
Public financial support
209 thou. CZK
Other public sources
450 thou. CZK
Non public and foreign sources
0 thou. CZK
Basic information
Recognised costs
359 CZK thou.
Public support
209 CZK thou.
58%
Provider
Czech Science Foundation
CEP
CE - Biochemistry
Solution period
01. 01. 2002 - 01. 01. 2004