1BK6
KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS
Summary for 1BK6
Entry DOI | 10.2210/pdb1bk6/pdb |
Descriptor | KARYOPHERIN ALPHA, LARGE T ANTIGEN, ... (4 entities in total) |
Functional Keywords | protein transport, nls nuclear import, armadillo repeat containing protein, complex (protein transport-peptide), complex (protein transport-peptide) complex, complex (protein transport/peptide) |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Total number of polymer chains | 6 |
Total formula weight | 95998.19 |
Authors | Conti, E.,Uy, M.,Leighton, L.,Blobel, G.,Kuriyan, J. (deposition date: 1998-07-14, release date: 1999-01-13, Last modification date: 2024-04-03) |
Primary citation | Conti, E.,Uy, M.,Leighton, L.,Blobel, G.,Kuriyan, J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Cell(Cambridge,Mass.), 94:193-204, 1998 Cited by PubMed Abstract: Selective nuclear import is mediated by nuclear localization signals (NLSs) and cognate transport factors known as karyopherins or importins. Karyopherin alpha recognizes "classical" monopartite and bipartite NLSs. We report the crystal structure of a 50 kDa fragment of the 60 kDa yeast karyopherin alpha, in the absence and presence of a monopartite NLS peptide at 2.2 A and 2.8 A resolution, respectively. The structure shows a tandem array of ten armadillo repeats, organized in a right-handed superhelix of helices. Binding of the NLS peptide occurs at two sites within a helical surface groove that is lined by conserved residues. The structure reveals the determinants of NLS specificity and suggests a model for the recognition of bipartite NLSs. PubMed: 9695948DOI: 10.1016/S0092-8674(00)81419-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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