1NO8

SOLUTION STRUCTURE OF THE NUCLEAR FACTOR ALY RBD DOMAIN


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 92 
  • Conformers Submitted: 32 
  • Selection Criteria: Structures with the lowest energy and lowest constraint energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of the Nuclear Factor ALY: Insights into Post-Transcriptional Regulatory and mRNA Nuclear Export Processes

Perez-Alvarado, G.C.Martinez-Yamout, M.Allen, M.M.Grosschedl, R.Dyson, H.J.Wright, P.E.

(2003) Biochemistry 42: 7348-7357

  • DOI: https://doi.org/10.1021/bi034062o
  • Primary Citation of Related Structures:  
    1NO8

  • PubMed Abstract: 

    ALY is a ubiquitously expressed nuclear protein which interacts with proteins such as TAP that are involved in export of mRNA from the nucleus to the cytoplasm, as well as with proteins that bind the T cell receptor alpha gene enhancer. ALY has also been shown to bind mRNA and to co-localize in the nucleus with components of a multiprotein postsplicing complex that is deposited 20-24 nucleotides upstream of exon-exon junctions. ALY has a conserved RNA binding domain (RBD) flanked by Gly-Arg rich N-terminal and C-terminal sequences. We determined the solution structure of the RBD homology region in ALY by nuclear magnetic resonance methods. The RBD motif in ALY has a characteristic beta(1)alpha(1)beta(2)-beta(3)alpha(2)beta(4) fold, consisting of a beta sheet composed of four antiparallel beta strands and two alpha helices that pack on one face of the beta sheet. As in other RBD structures, the beta sheet has an exposed face with hydrophobic and charged residues that could modulate interactions with other molecules. The loop that connects beta strands 2 and 3 is in intermediate motion in the NMR time scale, which is also characteristic of other RBDs. This loop presents side chains close to the exposed surface of the beta sheet and is a primary candidate site for intermolecular interactions. The structure of the conserved RBD of ALY provides insight into the nature of interactions involving this multifunctional protein.


  • Organizational Affiliation

    Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ALY106Mus musculusMutation(s): 0 
Gene Names: ALY
UniProt
Find proteins for O08583 (Mus musculus)
Explore O08583 
Go to UniProtKB:  O08583
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO08583
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 92 
  • Conformers Submitted: 32 
  • Selection Criteria: Structures with the lowest energy and lowest constraint energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-08-12
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Data collection, Database references, Derived calculations