1eaz
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(New page: 200px<br /> <applet load="1eaz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eaz, resolution 1.4Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 15:26, 29 October 2007
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CRYSTAL STRUCTURE OF THE PHOSPHOINOSITOL (3,4)-BISPHOSPHATE BINDING PH DOMAIN OF TAPP1 FROM HUMAN.
Overview
Phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] and its, immediate breakdown product PtdIns(3,4)P(2) function as second messengers, in growth factor- and insulin-induced signalling pathways. One of the ways, that these 3-phosphoinositides are known to regulate downstream signalling, events is by attracting proteins that possess specific PtdIns-binding, pleckstrin homology (PH) domains to the plasma membrane. Many of these, proteins, such as protein kinase B, phosphoinositide-dependent kinase 1, and the dual adaptor for phosphotyrosine and 3-phosphoinositides (DAPP1), interact with both PtdIns(3,4,5)P(3) and PtdIns(3,4)P(2) with similar, affinity. Recently, a new PH-domain-containing protein, termed tandem, PH-domain-containing protein (TAPP) 1, was described which is the ... [(full description)]
About this Structure
1EAZ is a [Single protein] structure of sequence from [Homo sapiens] with CIT as [ligand]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the phosphatidylinositol 3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): molecular basis of lipid specificity., Thomas CC, Dowler S, Deak M, Alessi DR, van Aalten DM, Biochem J. 2001 Sep 1;358(Pt 2):287-94. PMID:11513726
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