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2H4M

Karyopherin Beta2/Transportin-M9NLS

Summary for 2H4M
Entry DOI10.2210/pdb2h4m/pdb
Related1QBK
DescriptorTransportin-1, Heterogeneous nuclear ribonucleoprotein A1 (2 entities in total)
Functional Keywordsheat repeat, nuclear import complex, protein transport
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm: Q92973
Nucleus . Cytoplasm : P09651
Total number of polymer chains4
Total formula weight206204.67
Authors
Chook, Y.M.,Cansizoglu, A.E. (deposition date: 2006-05-24, release date: 2006-10-24, Last modification date: 2024-10-09)
Primary citationLee, B.J.,Cansizoglu, A.E.,Louis, T.H.,Zhang, Z.,Chook, Y.M.
Rules for nuclear localization sequence recognition by karyopherin beta 2.
Cell(Cambridge,Mass.), 126:543-558, 2006
Cited by
PubMed Abstract: Karyopherinbeta (Kapbeta) proteins bind nuclear localization and export signals (NLSs and NESs) to mediate nucleocytoplasmic trafficking, a process regulated by Ran GTPase through its nucleotide cycle. Diversity and complexity of signals recognized by Kap betas have prevented prediction of new Kap beta substrates. The structure of Kap beta 2 (also known as Transportin) bound to one of its substrates, the NLS of hnRNP A1, that we report here explains the mechanism of substrate displacement by Ran GTPase. Further analyses reveal three rules for NLS recognition by Kap beta 2: NLSs are structurally disordered in free substrates, have overall basic character, and possess a central hydrophobic or basic motif followed by a C-terminal R/H/KX(2-5)PY consensus sequence. We demonstrate the predictive nature of these rules by identifying NLSs in seven previously known Kap beta 2 substrates and uncovering 81 new candidate substrates, confirming five experimentally. These studies define and validate a new NLS that could not be predicted by primary sequence analysis alone.
PubMed: 16901787
DOI: 10.1016/j.cell.2006.05.049
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.05 Å)
Structure validation

238895

數據於2025-07-16公開中

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