4i0o | pdb_00004i0o
Nucleoporin ELYS (aa1-494), Mus musculus
Structural highlights
FunctionELYS_MOUSE Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis (By similarity). Has also been proposed to function as a transcription factor which may play a specific role in hematopoietic tissues (PubMed:11952839).[1] Publication Abstract from PubMedIn metazoa, the nuclear envelope (NE), together with the embedded nuclear pore complexes (NPCs), breaks down and reassembles during cell division. It is suggested that ELYS, a nucleoporin, binds to chromatin in an initial step of postmitotic NPC assembly and subsequently recruits the essential Y-subcomplex, the major scaffolding unit of the NPC. Here, we show that ELYS contains three domains: an N-terminal beta-propeller domain, a central alpha-helical domain, and a C-terminal disordered region. While the disordered region is responsible for the interactions with chromatin, the two preceding domains synergistically mediate tethering to the NPC. We present the crystal structure of the seven-bladed beta-propeller domain at 1.9 A resolution. Analysis of the beta-propeller surface reveals the regions that are required for NPC anchorage. We discuss the possible roles of ELYS in the context of the NPC scaffold architecture. Structural and Functional Studies of the 252 kDa Nucleoporin ELYS Reveal Distinct Roles for Its Three Tethered Domains.,Bilokapic S, Schwartz TU Structure. 2013 Apr 2;21(4):572-80. doi: 10.1016/j.str.2013.02.006. Epub 2013 Mar, 14. PMID:23499022[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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