Allain, Frédéric

Dominguez, Cyril

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Letters to the EditorBackbone resonance assignments for the Fv fragment of catalytic antibody 6D9 complexed with a transitionstate analogueDOI 10.1007/s10858-005-3870-xThe catalytic antibody 6D9, which was induced by immunization with chloramphenicol phosphonate(a transition-state analogue, TSA, for the reaction), catalyzes the hydrolysis of a non-bioactive chloram-phenicol monoester to generate the chloramphenicol (Miyashita et al., 1993). To understand the structure-catalytic activity relations of 6D9, we carried out NMR analyses of an Fv fragment of 6D9, which consistsof a 114-residue light chain (VL) and a 122-residue heavy chain (VH), complexed with TSA. For theassignments 2D and 3D heteronuclear NMR experiments with VL- and VH-selectively2H/13C/15N labeledFvs were used. The extent of backbone resonance assignments is 99% and 84% for VL and VH, respectively.BMRB deposit with accession number 6785.Reference: Miyashita et al. (1993) Proc. Natl. Acad. Sci. USA, 90, 5337–5340.Masayoshi Sakakuraa, Hideo Takahashib, Hiroaki Terasawaa, Kou Takeuchia, Ikuo Fujiic &Ichio Shimadaa,b,*aGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, 113-0033,Japan; bBiological Information Research Center (BIRC), National Institute of Advanced Industrial Scienceand Technology (AIST), Aomi, Koto-ku, Tokyo, 135-0064, Japan; cOsaka Prefecture University, Gakuen-cho,Sakai, Osaka, 599-8231, Japan*To whom correspondence should be addressed. E-mail: shimada@iw-nmr.f.u-tokyo.ac.jpSupplementary material is available in electronic format at http://dx.doi.org/10.1007/s10858-005-3870-xResonance assignments of the two N-terminal RNA recognition motifs (RRM) of the human heterogeneousnuclear ribonucleoprotein F (HnRNP F)DOI 10.1007/s10858-005-4287-2HnRNP F is a 45 kDa protein containing two N-terminal and one central RRM domains (Honore et al.,1995). It recognizes speciﬁcally poly-G RNA sequences (G-tracts) that are frequent cis-acting elementsimportant for splicing regulation (Grabowski, 2004). Mutations in HnRNP F binding sites have beencorrelated with many diseases. We initiated a structural study of a complex between HnRNP F and RNAcontaining G-tracts using NMR spectroscopy and decided to focus on the two N-terminal RRM domainsof HnRNP F (residues 1-194). Almost all 15N, 13C and 1H atoms have been assigned, except a few residueslocated at the N-terminus. In total, 94% of all observable atoms were assigned. The backbone and side-chain chemical shifts have been deposited in the BioMagResBank database (accession number 6745).References: Grabowski (2004) Biochem. Soc. Trans., 32, 924–927: Honore et al. (1995) J. Biol. Chem., 270,28780–28789.Cyril Dominguez & Fre´de´ric H.-T. Allain*Institute of Molecular Biology and Biophysics, Swiss Federal Institute of Technology Zu¨rich, ETH-Ho¨ng-gerberg, CH-8093, Zu¨rich*To whom correspondence should be addressed. E-mail: allain@mol.biol.ethz.chSupplementary material is available in electronic format at http://dx.doi.org/10.1007/s10858-005-4287-2Journal of Biomolecular NMR (2005) 33: 282  Springer 2005

Resonance Assignments of the Two N-terminal RNA Recognition Motifs (RRM) of the Human Heterogeneous Nuclear Ribonucleoprotein F (HnRNP F)

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Resonance Assignments of the Two N-terminal RNA Recognition Motifs (RRM) of the Human Heterogeneous Nuclear Ribonucleoprotein F (HnRNP F)

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