1EE5

YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A NUCLEOPLASMIN NLS PEPTIDE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.241 

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This is version 1.4 of the entry. See complete history. 


Literature

Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha.

Conti, E., Kuriyan, J.

(2000) Structure 8: 329-338

  • DOI: https://doi.org/10.1016/s0969-2126(00)00107-6
  • Primary Citation of Related Structures:  
    1EE4, 1EE5

  • PubMed Abstract: 

    Karyopherin alpha (importin alpha) is an adaptor molecule that recognizes proteins containing nuclear localization signals (NLSs). The prototypical NLS that is able to bind to karyopherin alpha is that of the SV40 T antigen, and consists of a short positively charged sequence motif. Distinct classes of NLSs (monopartite and bipartite) have been identified that are only partly conserved with respect to one another but are nevertheless recognized by the same receptor.

    • Organizational Affiliation: 

    Laboratory of Molecular Biophysics, Howard Hughes Medical Institute, The Rockefeller University, New York 10021, USA. conti@embl-heidelberg.de


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
KARYOPHERIN ALPHA424Saccharomyces cerevisiaeMutation(s): 1 
UniProt
Find proteins for Q02821 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q02821 
Go to UniProtKB:  Q02821
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ02821
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEOPLASMIN19Xenopus laevisMutation(s): 0 
UniProt
Find proteins for P05221 (Xenopus laevis)
Explore P05221 
Go to UniProtKB:  P05221
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP05221
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.241 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 157.56α = 90
b = 63.7β = 97.34
c = 62.15γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

  • Released Date: 2000-03-29 
    • Deposition Author(s): Conti, E.

Revision History  (Full details and data files)

  • Version 1.0: 2000-03-29
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Database references
  • Version 1.4: 2024-02-07
    Changes: Data collection