2L1L
NMR Solution Structure of the Phi0 PKI NES Peptide in Complex with CRM1-RanGTP
Summary for 2L1L
| Entry DOI | 10.2210/pdb2l1l/pdb |
| Descriptor | cAMP-dependent protein kinase inhibitor alpha, Exportin-1 (2 entities in total) |
| Functional Keywords | nuclear export, pki nes, crm1, rangtp, nuclear protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm: O14980 |
| Total number of polymer chains | 2 |
| Total formula weight | 17562.32 |
| Authors | Madl, T.,Sattler, M. (deposition date: 2010-07-29, release date: 2011-06-15, Last modification date: 2024-05-01) |
| Primary citation | Guttler, T.,Madl, T.,Neumann, P.,Deichsel, D.,Corsini, L.,Monecke, T.,Ficner, R.,Sattler, M.,Gorlich, D. NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Nat.Struct.Mol.Biol., 17:1367-1376, 2010 Cited by PubMed Abstract: Classic nuclear export signals (NESs) confer CRM1-dependent nuclear export. Here we present crystal structures of the RanGTP-CRM1 complex alone and bound to the prototypic PKI or HIV-1 Rev NESs. These NESs differ markedly in the spacing of their key hydrophobic (Φ) residues, yet CRM1 recognizes them with the same rigid set of five Φ pockets. The different Φ spacings are compensated for by different conformations of the bound NESs: in the case of PKI, an α-helical conformation, and in the case of Rev, an extended conformation with a critical proline docking into a Φ pocket. NMR analyses of CRM1-bound and CRM1-free PKI NES suggest that CRM1 selects NES conformers that pre-exist in solution. Our data lead to a new structure-based NES consensus, and explain why NESs differ in their affinities for CRM1 and why supraphysiological NESs bind the exportin so tightly. PubMed: 20972448DOI: 10.1038/nsmb.1931 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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