This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2k85
From Proteopedia
| Line 1: | Line 1: | ||
{{Seed}} | {{Seed}} | ||
| - | [[Image:2k85. | + | [[Image:2k85.png|left|200px]] |
<!-- | <!-- | ||
| Line 20: | Line 20: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2K85 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full | + | 2K85 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K85 OCA]. |
==Reference== | ==Reference== | ||
| Line 45: | Line 45: | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 17 09:00:01 2009'' |
Revision as of 06:00, 17 June 2009
p190-A RhoGAP FF1 domain
Template:ABSTRACT PUBMED 19393245
About this Structure
2K85 is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Bonet R, Ruiz L, Aragon E, Martin-Malpartida P, Macias MJ. NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding. J Mol Biol. 2009 Jun 5;389(2):230-7. Epub 2009 Apr 22. PMID:19393245 doi:10.1016/j.jmb.2009.04.035
Page seeded by OCA on Wed Jun 17 09:00:01 2009
Categories: Homo sapiens | Bonet, R. | Macias, M. | Martin-Malpartida, P. | Ruiz, L. | Alternative splicing | Anti-oncogene | Cell cycle | Cytoplasm | Dna-binding | Ff domain | Gtpase activation | Nucleus | P190-a rhogap | Phosphoprotein | Protein binding | Protein phosphorylation | Repressor | Transcription | Transcription regulation
