1AUD

U1A-UTRRNA, NMR, 31 STRUCTURES

Replaces:  1NUM

Summary for 1AUD

• Entry DOI: 10.2210/pdb1aud/pdb
• Descriptor: RNA 3UTR, U1A 102 (2 entities in total)
• Functional Keywords: complex (ribonucleoprotein-rna), rnp domain, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 21210.32

Authors

Allain, F.H.-T.,Gubser, C.C.,Howe, P.W.A.,Nagai, K.,Neuhaus, D.,Varani, G. (deposition date: 1997-08-22, release date: 1998-02-25, Last modification date: 2024-05-22)

Primary citation

Allain, F.H.,Howe, P.W.,Neuhaus, D.,Varani, G.
Structural basis of the RNA-binding specificity of human U1A protein.
EMBO J., 16:5764-5774, 1997

PubMed Abstract: The RNP domain is a very common eukaryotic protein domain involved in recognition of a wide range of RNA structures and sequences. Two structures of human U1A in complex with distinct RNA substrates have revealed important aspects of RNP-RNA recognition, but have also raised intriguing questions concerning the origin of binding specificity. The beta-sheet of the domain provides an extensive RNA-binding platform for packing aromatic RNA bases and hydrophobic protein side chains. However, many interactions between functional groups on the single-stranded nucleotides and residues on the beta-sheet surface are potentially common to RNP proteins with diverse specificity and therefore make only limited contribution to molecular discrimination. The refined structure of the U1A complex with the RNA polyadenylation inhibition element reported here clarifies the role of the RNP domain principal specificity determinants (the variable loops) in molecular recognition. The most variable region of RNP proteins, loop 3, plays a crucial role in defining the global geometry of the intermolecular interface. Electrostatic interactions with the RNA phosphodiester backbone involve protein side chains that are unique to U1A and are likely to be important for discrimination. This analysis provides a novel picture of RNA-protein recognition, much closer to our current understanding of protein-protein recognition than that of DNA-protein recognition.

PubMed: 9312034
DOI: 10.1093/emboj/16.18.5764

Experimental method

SOLUTION NMR