1fb8: Difference between revisions
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'''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH''' | '''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH''' | ||
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[[Category: Skolnik, E Y.]] | [[Category: Skolnik, E Y.]] | ||
[[Category: 3-phosphoinositide]] | [[Category: 3-phosphoinositide]] | ||
[[Category: | [[Category: Adaptor protein]] | ||
[[Category: | [[Category: Inositol tetrakisphosphate signal transduction protein]] | ||
[[Category: | [[Category: Pleckstrin]] | ||
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Revision as of 13:07, 2 May 2008
STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM DAPP1/PHISH
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
1FB8 is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Fri May 2 16:07:32 2008
