3LWW

Structure of an open and closed conformation of Human Importin Beta bound to the Snurportin1 IBB-domain trapped in the same crystallographic asymmetric unit

Summary for 3LWW

Entry DOI	10.2210/pdb3lww/pdb
Descriptor	Importin subunit beta-1, Snurportin-1 (2 entities in total)
Functional Keywords	protein transport, heat repeat, ibb-domain, importin beta, karyopherin, snurportin
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm: Q14974 Nucleus: O95149
Total number of polymer chains	4
Total formula weight	204571.13
Authors	Bhardwaj, A.,Cingolani, G. (deposition date: 2010-02-24, release date: 2010-06-02, Last modification date: 2023-09-06)
Primary citation	Bhardwaj, A.,Cingolani, G. Conformational selection in the recognition of the snurportin importin beta binding domain by importin beta. Biochemistry, 49:5042-5047, 2010 Cited by PubMed Abstract: The structural flexibility of beta-karyopherins is critical to mediate the interaction with transport substrates, nucleoporins, and the GTPase Ran. In this paper, we provide structural evidence that the molecular recognition of the transport adaptor snurportin by importin beta follows the population selection mechanism. We have captured two drastically different conformations of importin beta bound to the snurportin importin beta binding domain trapped in the same crystallographic asymmetric unit. We propose the population selection may be a general mechanism used by beta-karyopherins to recognize transport substrates. PubMed: 20476751 DOI: 10.1021/bi100292y PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.15 Å)

Structure validation