1fvr
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1fvr.gif|left|200px]] | [[Image:1fvr.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1fvr", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1fvr| PDB=1fvr | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''TIE2 KINASE DOMAIN''' | '''TIE2 KINASE DOMAIN''' | ||
Line 35: | Line 32: | ||
[[Category: Moore, J T.]] | [[Category: Moore, J T.]] | ||
[[Category: Shewchuk, L M.]] | [[Category: Shewchuk, L M.]] | ||
- | [[Category: | + | [[Category: Tyrosine kinase]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:49:04 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 13:49, 2 May 2008
TIE2 KINASE DOMAIN
Overview
BACKGROUND: Angiogenesis, the formation of new vessels from the existing vasculature, is a critical process during early development as well as in a number of disease processes. Tie2 (also known as Tek) is an endothelium-specific receptor tyrosine kinase involved in both angiogenesis and vasculature maintenance. RESULTS: We have determined the crystal structure of the Tie2 kinase domain to 2.2 A resolution. The structure contains the catalytic core, the kinase insert domain (KID), and the C-terminal tail. The overall fold is similar to that observed in other serine/threonine and tyrosine kinase structures; however, several unique features distinguish the Tie2 structure from those of other kinases. The Tie2 nucleotide binding loop is in an inhibitory conformation, which is not seen in other kinase structures, while its activation loop adopts an "activated-like" conformation in the absence of phosphorylation. Tyr-897, located in the N-terminal domain, may negatively regulate the activity of Tie2 by preventing dimerization of the kinase domains or by recruiting phosphatases when it is phosphorylated. CONCLUSION: Regulation of the kinase activity of Tie2 is a complex process. Conformational changes in the nucleotide binding loop, activation loop, C helix, and the C-terminal tail are required for ATP and substrate binding.
About this Structure
1FVR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the Tie2 RTK domain: self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail., Shewchuk LM, Hassell AM, Ellis B, Holmes WD, Davis R, Horne EL, Kadwell SH, McKee DD, Moore JT, Structure. 2000 Nov 15;8(11):1105-13. PMID:11080633 Page seeded by OCA on Fri May 2 16:49:04 2008