| dc.contributor |
Carla Mattos, Committee Chair |
|
| dc.contributor |
Clay Clark, Committee Member |
|
| dc.contributor |
Robert Rose, Committee Member |
|
| dc.creator |
Miller, Christopher Michael |
|
| dc.date |
2010-04-02T18:17:41Z |
|
| dc.date |
2010-04-02T18:17:41Z |
|
| dc.date |
2007-01-21 |
|
| dc.date.accessioned |
2023-02-27T12:15:52Z |
|
| dc.date.available |
2023-02-27T12:15:52Z |
|
| dc.identifier |
etd-08142006-074018 |
|
| dc.identifier |
http://www.lib.ncsu.edu/resolver/1840.16/2819 |
|
| dc.identifier.uri |
http://localhost:8080/xmlui/handle/CUHPOERS/262621 |
|
| dc.description |
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. |
|
| 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. |
|
| dc.subject |
x-ray crystallography |
|
| dc.subject |
Rap1a |
|
| dc.subject |
GTPase |
|
| dc.subject |
Ras superfamily |
|
| dc.subject |
protein |
|
| dc.title |
1.9A Crystal Structure of the Rap1a GTPase Bound to its Natural Ligand, GTP |
|