(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)

Stéphanie Cabal; Carine van Heijenoort; Eric Guittet

doi:10.1007/s12104-007-9061-9

(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)

Biomol NMR Assign. 2007 Dec;1(2):221-3. doi: 10.1007/s12104-007-9061-9. Epub 2007 Nov 3.

Authors

Stéphanie Cabal¹, Carine van Heijenoort, Eric Guittet

Affiliation

¹ ICSN-CNRS, Gif sur Yvette, France.

PMID: 19636870
DOI: 10.1007/s12104-007-9061-9

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Motifs
Amino Acid Sequence
Carbon Isotopes / chemistry
Heterogeneous-Nuclear Ribonucleoprotein Group F-H / chemistry*
Humans
Magnetic Resonance Spectroscopy / methods*
Molecular Weight
Nitrogen Isotopes / chemistry
Protein Binding
Protein Structure, Tertiary
Protons
RNA / chemistry*

Substances

Carbon Isotopes
Heterogeneous-Nuclear Ribonucleoprotein Group F-H
Nitrogen Isotopes
Protons
RNA