1fhx
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(New page: 200px<br /><applet load="1fhx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fhx, resolution 2.50Å" /> '''Structure of the ple...)
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Revision as of 12:49, 20 November 2007
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Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate
Overview
Pleckstrin homology (PH) domains are protein modules of around 120 amino, acids found in many proteins involved in cellular signaling. Certain PH, domains drive signal-dependent membrane recruitment of their host proteins, by binding strongly and specifically to lipid second messengers produced, by agonist-stimulated phosphoinositide 3-kinases (PI 3-Ks). We describe, X-ray crystal structures of two different PH domains bound to, Ins(1,3,4,5)P4, the head group of the major PI 3-K product, PtdIns(3,4,5)P3. One of these PH domains (from Grp1) is PtdIns(3,4,5)P3, specific, while the other (from DAPP1/PHISH) binds strongly to both, PtdIns(3,4,5)P3 and its 5'-dephosphorylation product, PtdIns(3,4)P2., Comparison of the two structures provides an explanation for the distinct, phosphoinositide specificities of the two PH domains and allows us to, predict the 3-phosphoinositide selectivity of uncharacterized PH domains.
About this Structure
1FHX is a Single protein structure of sequence from Mus musculus with SO4 and 4IP as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains., Ferguson KM, Kavran JM, Sankaran VG, Fournier E, Isakoff SJ, Skolnik EY, Lemmon MA, Mol Cell. 2000 Aug;6(2):373-84. PMID:10983984
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