5hb4: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/NU192_CHATD NU192_CHATD] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs.[UniProtKB:P47054]
[https://www.uniprot.org/uniprot/NU192_CHATD NU192_CHATD] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs.[UniProtKB:P47054]
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== Publication Abstract from PubMed ==
The nuclear pore complex (NPC) controls the transport of macromolecules between the nucleus and cytoplasm, but its molecular architecture has thus far remained poorly defined. We biochemically reconstituted NPC core protomers and elucidated the underlying protein-protein interaction network. Flexible linker sequences, rather than interactions between the structured core scaffold nucleoporins, mediate the assembly of the inner ring complex and its attachment to the NPC coat. X-ray crystallographic analysis of these scaffold nucleoporins revealed the molecular details of their interactions with the flexible linker sequences and enabled construction of full-length atomic structures. By docking these structures into the cryoelectron tomographic reconstruction of the intact human NPC and validating their placement with our nucleoporin interactome, we built a composite structure of the NPC symmetric core that contains ~320,000 residues and accounts for ~56 megadaltons of the NPC's structured mass. Our approach provides a paradigm for the structure determination of similarly complex macromolecular assemblies.
Architecture of the symmetric core of the nuclear pore.,Lin DH, Stuwe T, Schilbach S, Rundlet EJ, Perriches T, Mobbs G, Fan Y, Thierbach K, Huber FM, Collins LN, Davenport AM, Jeon YE, Hoelz A Science. 2016 Apr 15;352(6283):aaf1015. doi: 10.1126/science.aaf1015. Epub 2016, Apr 14. PMID:27081075<ref>PMID:27081075</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
*[[Nucleoporin 3D structures|Nucleoporin 3D structures]]
== References ==
<references/>
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Latest revision as of 15:31, 6 March 2024

Crystal structure of Chaetomium thermophilum Nup192Crystal structure of Chaetomium thermophilum Nup192

Structural highlights

5hb4 is a 1 chain structure with sequence from Chaetomium thermophilum and Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NU192_CHATD Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs.[UniProtKB:P47054]

See Also

5hb4, resolution 3.20Å

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OCA
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