PDBsum entry 1l3k

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protein links
RNA binding protein PDB id
Protein chain
163 a.a. *
Waters ×227
* Residue conservation analysis
PDB id:
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
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
27-Feb-02     Release date:   17-Apr-02    
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Protein chain
Pfam   ArchSchema ?
P09651  (ROA1_HUMAN) -  Heterogeneous nuclear ribonucleoprotein A1
372 a.a.
163 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     nucleotide binding     2 terms  


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.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19667073 H.L.Okunola, and A.R.Krainer (2009).
Cooperative-binding and splicing-repressive properties of hnRNP A1.
  Mol Cell Biol, 29, 5620-5631.  
17188295 K.R.Thickman, E.A.Sickmier, and C.L.Kielkopf (2007).
Alternative conformations at the RNA-binding surface of the N-terminal U2AF(65) RNA recognition motif.
  J Mol Biol, 366, 703-710.
PDB code: 2hzc
17375936 M.C.Swenson, S.R.Paranawithana, P.S.Miller, and C.L.Kielkopf (2007).
Structure of a DNA repair substrate containing an alkyl interstrand cross-link at 1.65 A resolution.
  Biochemistry, 46, 4545-4553.
PDB code: 2oks
16818232 E.A.Sickmier, K.E.Frato, H.Shen, S.R.Paranawithana, M.R.Green, and C.L.Kielkopf (2006).
Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65.
  Mol Cell, 23, 49-59.
PDB codes: 2fzr 2g4b
15699629 G.V.Tolstonog, G.Li, R.L.Shoeman, and P.Traub (2005).
Interaction in vitro of type III intermediate filament proteins with higher order structures of single-stranded DNA, particularly with G-quadruplex DNA.
  DNA Cell Biol, 24, 85.  
15206938 M.Nakanishi, A.Yoshimura, N.Ishida, Y.Ueno, and Y.Kitade (2004).
Contribution of Tyr712 and Phe716 to the activity of human RNase L.
  Eur J Biochem, 271, 2737-2744.  
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