1fvr

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{{STRUCTURE_1fvr| PDB=1fvr | SCENE= }}
{{STRUCTURE_1fvr| PDB=1fvr | SCENE= }}
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'''TIE2 KINASE DOMAIN'''
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===TIE2 KINASE DOMAIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11080633 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11080633}}
==About this Structure==
==About this Structure==
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[[Category: Shewchuk, L M.]]
[[Category: Shewchuk, L M.]]
[[Category: Tyrosine kinase]]
[[Category: Tyrosine kinase]]
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Revision as of 01:00, 1 July 2008

Template:STRUCTURE 1fvr

TIE2 KINASE DOMAIN

Template:ABSTRACT PUBMED 11080633

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

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