4a5k

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[[Image:4a5k.jpg|left|200px]]
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==Structural analyses of Slm1-PH domain demonstrate ligand binding in the non-canonical site==
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<StructureSection load='4a5k' size='340' side='right' caption='[[4a5k]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4a5k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A5K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A5K FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a6f|4a6f]], [[4a6h|4a6h]], [[4a6k|4a6k]]</td></tr>
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<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=4a5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a5k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a5k RCSB], [http://www.ebi.ac.uk/pdbsum/4a5k PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: Pleckstrin homology (PH) domains are common membrane-targeting modules and their best characterized ligands are a set of important signaling lipids that include phosphatidylinositol phosphates (PtdInsPs). PH domains recognize PtdInsPs through two distinct mechanisms that use different binding pockets on opposite sides of the beta-strands 1 and 2: i) a canonical binding site delimited by the beta1-beta2 and beta3-beta4loops and ii) a non-canonical binding site bordered by the beta1-beta2 and beta5-beta6loops. The PH domain-containing protein Slm1 from budding yeast Saccharomyces cerevisiae is required for actin cytoskeleton polarization and cell growth. We recently reported that this PH domain binds PtdInsPs and phosphorylated sphingolipids in a cooperative manner. PRINCIPAL FINDINGS: To study the structural basis for the Slm1-PH domain (Slm1-PH) specificity, we co-crystallized this domain with different soluble compounds that have structures analogous to anionic lipid head groups of reported Slm1 ligands: inositol 4-phosphate, which mimics phosphatidylinositol-4-phosphate (PtdIns(4)P), and phosphoserine as a surrogate for dihydrosphingosine 1-phosphate (DHS1-P). We found electron densities for the ligands within the so-called non-canonical binding site. An additional positively charged surface that contacts a phosphate group was identified next to the canonical binding site. CONCLUSIONS: Our results suggest that Slm1-PH utilizes a non-canonical binding site to bind PtdInsPs, similar to that described for the PH domains of beta-spectrin, Tiam1 and ArhGAP9. Additionally, Slm1-PH may have retained an active canonical site. We propose that the presence of both a canonical and a non-canonical binding pocket in Slm1-PH may account for the cooperative binding to PtdInsPs and DHS-1P.
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Structural Analyses of the Slm1-PH Domain Demonstrate Ligand Binding in the Non-Canonical Site.,Anand K, Maeda K, Gavin AC PLoS One. 2012;7(5):e36526. Epub 2012 May 4. PMID:22574179<ref>PMID:22574179</ref>
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{{STRUCTURE_4a5k| PDB=4a5k | SCENE= }}
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===Structural analyses of Slm1-PH domain demonstrate ligand binding in the non-canonical site===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_22574179}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 22574179 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_22574179}}
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==About this Structure==
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[[4a5k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A5K OCA].
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==Reference==
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<ref group="xtra">PMID:022574179</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Anand, K.]]
[[Category: Anand, K.]]

Revision as of 08:20, 5 June 2014

Structural analyses of Slm1-PH domain demonstrate ligand binding in the non-canonical site

4a5k, resolution 1.76Å

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