Structural and biochemical characterization of nuclear pore complex structural scaffold sub-complexes

The nuclear pore complex (NPC) is a large, modular protein assembly that regulates nucleocytoplasmic transport in all eukaryotes. The ~60-120 MDa NPC is a modular assembly of multiple copies of ~30 distinct proteins that are arranged into biochemically distinct sub-complexes. We believe that the structural characterization of the NPC is essential for understanding its transport mechanisms and various pathologies and human diseases associated with deletions or mutations of constituents. To obtain detailed structural information of the NPC, techniques that span several resolution ranges are necessary due to its large size and complexity. For instance, recent progress in the structural characterization of the overall architecture of the NPC by cryo-electron tomography(cryo-ET) to ~23Å resolution has revealed its size, shape, and course arrangement, but lacks distinguishable protein-protein boundaries and secondary structural details.

Department dc:contributor.department

Massachusetts Institute of Technology. Department of Biology

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2017

Author dc:creator

• Kelley, Kotaro.

Advisor dc:contributor.advisor

• Thomas U. Schwartz.

• Biology.

Statement dc:rights

• MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/113466

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/113466