1EE4

CRYSTAL STRUCTURE OF YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A C-MYC NLS PEPTIDE

Summary for 1EE4

• Entry DOI: 10.2210/pdb1ee4/pdb
• Related: 1BK6 1EE5
• Descriptor: KARYOPHERIN ALPHA, MYC PROTO-ONCOGENE PROTEIN (3 entities in total)
• Functional Keywords: arm repeat, transport protein
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm, perinuclear region: Q02821; Nucleus, nucleoplasm: P01106
• Total number of polymer chains: 6
• Total formula weight: 97741.91

Authors

Conti, E. (deposition date: 2000-01-30, release date: 2000-03-29, Last modification date: 2024-02-07)

Primary citation

Conti, E.,Kuriyan, J.
Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha.
Structure Fold.Des., 8:329-338, 2000

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.

PubMed: 10745017
DOI: 10.1016/S0969-2126(00)00107-6

Experimental method

X-RAY DIFFRACTION (2.1 Å)