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1PJM

Mouse Importin alpha-bipartite NLS from human retinoblastoma protein Complex

Summary for 1PJM
Entry DOI10.2210/pdb1pjm/pdb
Related1EJL 1EJY 1IQ1
DescriptorRetinoblastoma-associated protein, Importin alpha-2 subunit (3 entities in total)
Functional Keywordsimportin alpha/karyopherin alpha, nuclear localization sequence (nls) recognition, bipartite nls, human retinoblastoma protein, protein transport
Biological sourceMus musculus (house mouse)
More
Cellular locationNucleus: P06400
Cytoplasm (By similarity): P52293
Total number of polymer chains2
Total formula weight52016.16
Authors
Fontes, M.R.M.,Teh, T.,Jans, D.,Brinkworth, R.I.,Kobe, B. (deposition date: 2003-06-03, release date: 2003-08-19, Last modification date: 2023-08-16)
Primary citationFontes, M.R.M.,Teh, T.,Jans, D.,Brinkworth, R.I.,Kobe, B.
Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha
J.Biol.Chem., 278:27981-27987, 2003
Cited by
PubMed Abstract: Importin-alpha is the nuclear import receptor that recognizes cargo proteins carrying conventional basic monopartite and bipartite nuclear localization sequences (NLSs) and facilitates their transport into the nucleus. Bipartite NLSs contain two clusters of basic residues, connected by linkers of variable lengths. To determine the structural basis of the recognition of diverse bipartite NLSs by mammalian importin-alpha, we co-crystallized a non-autoinhibited mouse receptor protein with peptides corresponding to the NLSs from human retinoblastoma protein and Xenopus laevis phosphoprotein N1N2, containing diverse sequences and lengths of the linker. We show that the basic clusters interact analogously in both NLSs, but the linker sequences adopt different conformations, whereas both make specific contacts with the receptor. The available data allow us to draw general conclusions about the specificity of NLS binding by importin-alpha and facilitate an improved definition of the consensus sequence of a conventional basic/bipartite NLS (KRX10-12KRRK) that can be used to identify novel nuclear proteins.
PubMed: 12695505
DOI: 10.1074/jbc.M303275200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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数据于2024-11-13公开中

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