1994
DOI: 10.1002/j.1460-2075.1994.tb06698.x
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: The RNP domain is a very common motif found in hundreds of proteins, including many protein components of the RNA processing machinery. The 70‐90 amino acid domain contains two highly conserved stretches of 6‐8 amino acids (RNP‐1 and RNP‐2) in the central strands of a four‐stranded antiparallel beta‐sheet, packed against two alpha‐helices by a conserved hydrophobic core. Using multidimensional heteronuclear NMR, we have mapped intermolecular contacts between the human U1A protein 102 amino acid N‐terminal RNP … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

3
59
0

Year Published

1995
1995
2010
2010

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 71 publications
(62 citation statements)
references
References 46 publications
3
59
0
Order By: Relevance
“…Tat and TAR interaction occurs in the deep A-form major groove of the RNA near the bulge [6,7]. Even a slightly widened major groove of the HIV-1 TAR, however, would be too narrow to accommodate an a-helical peptide [37,38].…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Tat and TAR interaction occurs in the deep A-form major groove of the RNA near the bulge [6,7]. Even a slightly widened major groove of the HIV-1 TAR, however, would be too narrow to accommodate an a-helical peptide [37,38].…”
Section: Discussionmentioning
confidence: 99%
“…Extended conformations are found at the recognition sites of both DNA minor groove binding proteins (TATA-box binding protein) [39,40] and RNA binding proteins [37,41,42] when steric requirements render the formation of co-helices disadvantageous. The DNA minor groove has a geometry comparable to that of the A-form RNA major groove.…”
Section: Discussionmentioning
confidence: 99%
“…It has been previously shown that the N-terminal RRM is solely responsible for the binding of U1A to U1 snRNA (19,21). To test whether this is also the case for IgM-(1790 -2085), we examined its affinity, relative to U1 snRNA, for the truncated version of U1A containing only amino acids 1-117, which span RRM1.…”
Section: Estimation Of Relative Binding Affinity Of Full-length U1a Amentioning
confidence: 99%
“…We have also shown that U1A binds this site via its N-terminal domain, the same as is used for binding to U1snRNP. Based on crystallographic and NMR studies of the interaction of the N-terminal domain of U1A with the consensus binding sites on U1snRNP and PIE RNA (19,21,22,24), it is possible to envision how U1A binds the novel sites. The bases of the consensus binding site, in particular the UGC of the AUUGCAC of the unpaired loop, stack with amino acid side chains within the ␤ sheet of the U1A protein via electrostatic interactions (see Protein data bank pdb accession number 1DZ5).…”
Section: Estimation Of Relative Binding Affinity Of Full-length U1a Amentioning
confidence: 99%
“…Others identify specific sequences through their relative flexibility that induces distortions in the DNA duplex (McClarin et al 1986;Kim et al 1993). RNA-binding proteins can recognize sequences through readout of the hydrogen bonding patterns of the bases on the Watson-Crick and Hoogsteen faces, or through shapespecific recognition of RNA secondary and tertiary structure (Howe et al 1994;Valegard et al 1994;Hudson et al 2004;Hall 2005).…”
Section: Introductionmentioning
confidence: 99%