5dh9
Crystal Structure of PKI NES Flip Mutant Peptide in complex with CRM1-Ran-RanBP1Crystal Structure of PKI NES Flip Mutant Peptide in complex with CRM1-Ran-RanBP1
Structural highlights
FunctionIPKA_HUMAN Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. Publication Abstract from PubMedThe Chromosome Region of Maintenance 1 (CRM1) protein mediates nuclear export of hundreds of proteins through recognition of their nuclear export signals (NESs), which are highly variable in sequence and structure. The plasticity of the CRM1-NES interaction is not well understood, as there are many NES sequences that seem incompatible with structures of the NES-bound CRM1 groove. Crystal structures of CRM1 bound to two different NESs with unusual sequences showed the NES peptides binding the CRM1 groove in the opposite orientation (minus) to that of previously studied NESs (plus). Comparison of minus and plus NESs identified structural and sequence determinants for NES orientation. The binding of NESs to CRM1 in both orientations results in a large expansion in NES consensus patterns and therefore a corresponding expansion of potential NESs in the proteome. Structural determinants of nuclear export signal orientation in binding to exportin CRM1.,Fung HY, Fu SC, Brautigam CA, Chook YM Elife. 2015 Sep 8;4. doi: 10.7554/eLife.10034. PMID:26349033[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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