1fhw: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fhw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FHW FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fhw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FHW FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I5P:INOSITOL-(1,3,4,5,6)-PENTAKISPHOSPHATE'>I5P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I5P:INOSITOL-(1,3,4,5,6)-PENTAKISPHOSPHATE'>I5P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fhx|1fhx]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fhx|1fhx]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fhw RCSB], [http://www.ebi.ac.uk/pdbsum/1fhw PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fhw RCSB], [http://www.ebi.ac.uk/pdbsum/1fhw PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Ferguson, K M | [[Category: Ferguson, K M]] | ||
[[Category: Fournier, E | [[Category: Fournier, E]] | ||
[[Category: Isakoff, S J | [[Category: Isakoff, S J]] | ||
[[Category: Kavran, J M | [[Category: Kavran, J M]] | ||
[[Category: Lemmon, M A | [[Category: Lemmon, M A]] | ||
[[Category: Sankaran, V G | [[Category: Sankaran, V G]] | ||
[[Category: Skolnik, E Y | [[Category: Skolnik, E Y]] | ||
[[Category: 3-phosphoinositide]] | [[Category: 3-phosphoinositide]] | ||
[[Category: Guanine nucleotide exchange factor]] | [[Category: Guanine nucleotide exchange factor]] | ||
Revision as of 03:26, 23 December 2014
Structure of the pleckstrin homology domain from GRP1 in complex with inositol(1,3,4,5,6)pentakisphosphateStructure of the pleckstrin homology domain from GRP1 in complex with inositol(1,3,4,5,6)pentakisphosphate
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPleckstrin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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