PDBsum entry 1l3k

RNA binding protein

PDB id: 1l3k

Contents

Protein chain

163 a.a. *

Waters ×227

* Residue conservation analysis

PDB id:

1l3k

Name:

RNA binding protein

Title:

Up1, the two RNA-recognition motif domain of hnrnp a1

Structure:

Heterogeneous nuclear ribonucleoprotein a1. Chain: a. Fragment: RNA-recognition motif domain. Synonym: hnrnp a1, up1, helix-destabilizing protein, single-strand binding protein, hnrnp core protein a1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.10Å R-factor: 0.156 R-free: 0.194

Authors:

J.Vitali,J.Ding,J.Jiang,Y.Zhang,A.R.Krainer,R.-M.Xu

Key ref:

J.Vitali et al. (2002). Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. Nucleic Acids Res, 30, 1531-1538. PubMed id: 11917013 DOI: 10.1093/nar/30.7.1531

Date:

27-Feb-02 Release date: 17-Apr-02

Protein chain

P09651  (ROA1_HUMAN) -  Heterogeneous nuclear ribonucleoprotein A1 from Homo sapiens

Seq: 372 a.a.

Struc: 163 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/nar/30.7.1531

Nucleic Acids Res 30:1531-1538 (2002)

PubMed id: 11917013

Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1.

J.Vitali, J.Ding, J.Jiang, Y.Zhang, A.R.Krainer, R.M.Xu.

ABSTRACT

The RNA-recognition motif (RRM) is a common and evolutionarily conserved RNA-binding module. Crystallographic and solution structural studies have shown that RRMs adopt a compact alpha/beta structure, in which four antiparallel beta-strands form the major RNA-binding surface. Conserved aromatic residues in the RRM are located on the surface of the beta-sheet and are important for RNA binding. To further our understanding of the structural basis of RRM-nucleic acid interaction, we carried out a high resolution analysis of UP1, the N-terminal, two-RRM domain of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1), whose structure was previously solved at 1.75-1.9 A resolution. The two RRMs of hnRNP A1 are closely related but have distinct functions in regulating alternative pre-mRNA splice site selection. Our present 1.1 A resolution crystal structure reveals that two conserved solvent-exposed phenylalanines in the first RRM have alternative side chain conformations. These conformations are spatially correlated, as the individual amino acids cannot adopt each of the observed conformations independently. These phenylalanines are critical for nucleic acid binding and the observed alternative side chain conformations may serve as a mechanism for regulating nucleic acid binding by RRM-containing proteins.