5ijo | pdb_00005ijo
Alternative composite structure of the inner ring of the human nuclear pore complex (16 copies of Nup188, 16 copies of Nup205)
Structural highlights
Disease[NUP62_HUMAN] Familial infantile bilateral striatal necrosis. The disease is caused by mutations affecting the gene represented in this entry. [NU155_HUMAN] Familial atrial fibrillation. The disease is caused by mutations affecting the gene represented in this entry. [NU188_HUMAN] Copy number variations of NUP188 gene may be a cause of heterotaxy, a congenital heart disease resulting from abnormalities in left-right (LR) body patterning.[1] Function[NUP62_HUMAN] Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex. [NUP54_HUMAN] Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. [NU155_HUMAN] Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.[UniProtKB:Q99P88] [NU205_HUMAN] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC.[2] [NU188_HUMAN] May function as a component of the nuclear pore complex (NPC). [NUP93_HUMAN] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC.[3] [4] [NUP58_HUMAN] Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. Publication Abstract from PubMedNuclear pore complexes (NPCs) are 110-megadalton assemblies that mediate nucleocytoplasmic transport. NPCs are built from multiple copies of ~30 different nucleoporins, and understanding how these nucleoporins assemble into the NPC scaffold imposes a formidable challenge. Recently, it has been shown how the Y complex, a prominent NPC module, forms the outer rings of the nuclear pore. However, the organization of the inner ring has remained unknown until now. We used molecular modeling combined with cross-linking mass spectrometry and cryo-electron tomography to obtain a composite structure of the inner ring. This architectural map explains the vast majority of the electron density of the scaffold. We conclude that despite obvious differences in morphology and composition, the higher-order structure of the inner and outer rings is unexpectedly similar. Molecular architecture of the inner ring scaffold of the human nuclear pore complex.,Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M Science. 2016 Apr 15;352(6283):363-5. doi: 10.1126/science.aaf0643. PMID:27081072[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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