(1)H, (13)C and (15)N resonance assignment of the first N-terminal RNA recognition motif (RRM) of the human heterogeneous nuclear ribonucleoprotein H (hnRNP H).
Human heterogeneous nuclear ribonucleoprotein H (hnRNP H) regulates alternative splicing of HIV-1 Tat pre-mRNA. The structure of the first N-terminal domain (residues 1-104) of hnRNP H was solved and its binding to an exonic splicing silencer (pESS2) studied. For this, all backbone and 85% of side-chain resonance frequencies were assigned.
Cabal
Stéphanie
S
ICSN-CNRS, Gif sur Yvette, France.
van Heijenoort
Carine
C
Guittet
Eric
E
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D034541:Heterogeneous-Nuclear Ribonucleoprotein Group F-H / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011522:Protons; D012313:RNA / Q000737:chemistry*
D002247:Carbon Isotopes; D034541:Heterogeneous-Nuclear Ribonucleoprotein Group F-H; D009587:Nitrogen Isotopes; D011522:Protons; D012313:RNA