1fhx
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1fhx |SIZE=350|CAPTION= <scene name='initialview01'>1fhx</scene>, resolution 2.50Å | |PDB= 1fhx |SIZE=350|CAPTION= <scene name='initialview01'>1fhx</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fhw|1FHW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhx OCA], [http://www.ebi.ac.uk/pdbsum/1fhx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fhx RCSB]</span> | ||
}} | }} | ||
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[[Category: Sankaran, V G.]] | [[Category: Sankaran, V G.]] | ||
[[Category: Skolnik, E Y.]] | [[Category: Skolnik, E Y.]] | ||
| - | [[Category: 4IP]] | ||
| - | [[Category: SO4]] | ||
[[Category: 3-phosphoinositide]] | [[Category: 3-phosphoinositide]] | ||
[[Category: guanine nucleotide exchange factor]] | [[Category: guanine nucleotide exchange factor]] | ||
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[[Category: pleckstrin]] | [[Category: pleckstrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:23:22 2008'' |
Revision as of 17:23, 30 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1FHW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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