1.9A Crystal Structure of the Rap1a GTPase Bound to its Natural Ligand, GTP

Show simple item record

dc.contributor.advisor Carla Mattos, Committee Chair en_US
dc.contributor.advisor Clay Clark, Committee Member en_US
dc.contributor.advisor Robert Rose, Committee Member en_US
dc.contributor.author Miller, Christopher Michael en_US
dc.date.accessioned 2010-04-02T18:17:41Z
dc.date.available 2010-04-02T18:17:41Z
dc.date.issued 2007-01-21 en_US
dc.identifier.other etd-08142006-074018 en_US
dc.identifier.uri http://www.lib.ncsu.edu/resolver/1840.16/2819
dc.description.abstract Rap1a is a small GTPase in the Ras superfamily whose most well known function is to antagonize the Ras. Rap1a and Ras share common effectors which allow Rap1a to either unproductively bind Ras' effectors forming an inactive complex or sequester Ras' effectors away from the plasma membrane where Ras is inserted by C-terminal post-translational modifications. To date, a 2.2Å crystal structure of Rap1a bound to the non-hydrolyzable GTP analogue, GMPPNP, and one of its effectors, Raf-1, has been solved. This thesis presents the 1.9Å monomeric form of Rap1a bound to its natural ligand, GTP. Comparisons made between the previously published Rap—Raf structure, Rap2a, H-Ras, and RalA shed some light on the functions for conserved areas of Rap1a. The presence of a unique salt bridge at the Rap⁄Raf interface, a new conformation of threonine 61, a possible link for switch the II residue phenylalanine 64 with GAP-induced GTPase activity, and a suggested role for α helix 4 contribute to the Rap1a story. en_US
dc.rights I hereby certify that, if appropriate, I have obtained and attached hereto a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee. I hereby grant to NC State University or its agents the non-exclusive license to archive and make accessible, under the conditions specified below, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report. en_US
dc.subject x-ray crystallography en_US
dc.subject Rap1a en_US
dc.subject GTPase en_US
dc.subject Ras superfamily en_US
dc.subject protein en_US
dc.title 1.9A Crystal Structure of the Rap1a GTPase Bound to its Natural Ligand, GTP en_US
dc.degree.name MS en_US
dc.degree.level thesis en_US
dc.degree.discipline Biochemistry en_US

Files in this item

Files Size Format View
etd.pdf 3.700Mb PDF View/Open

This item appears in the following Collection(s)

Show simple item record