1btn

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(New page: 200px<br /><applet load="1btn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1btn, resolution 2.0&Aring;" /> '''STRUCTURE OF THE BIND...)
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[[Image:1btn.gif|left|200px]]<br /><applet load="1btn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1btn, resolution 2.0&Aring;" />
 
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'''STRUCTURE OF THE BINDING SITE FOR INOSITOL PHOSPHATES IN A PH DOMAIN'''<br />
 
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==Overview==
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==STRUCTURE OF THE BINDING SITE FOR INOSITOL PHOSPHATES IN A PH DOMAIN==
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Phosphatidylinositol bisphosphate has been found to bind specifically to, pleckstrin homology (PH) domains that are commonly present in signalling, proteins but also found in cytoskeleton. We have studied the complexes of, the beta-spectrin PH domain and soluble inositol phosphates using both, circular dichroism and nuclear magnetic resonance spectroscopy, and X-ray, crystallography. The specific binding site is located in the centre of a, positively charged surface patch of the domain. The presence of, 4,5-bisphosphate group on the inositol ring is critical for binding. In, the crystal structure that has been determined at 2.0 A resolution, inositol-1,4,5-trisphosphate is bound with salt bridges and hydrogen bonds, through these phosphate groups whereas the 1-phosphate group is mostly, solvent-exposed and the inositol ring has virtually no interactions with, the protein. We propose a model in which PH domains are involved in, reversible anchoring of proteins to membranes via their specific binding, to phosphoinositides. They could also participate in a response to a, second messenger such as inositol trisphosphate, organizing cross-roads in, cellular signalling.
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<StructureSection load='1btn' size='340' side='right'caption='[[1btn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1btn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BTN FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1btn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1btn OCA], [https://pdbe.org/1btn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1btn RCSB], [https://www.ebi.ac.uk/pdbsum/1btn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1btn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SPTB2_MOUSE SPTB2_MOUSE] Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bt/1btn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1btn ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with I3P as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BTN OCA].
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*[[Spectrin 3D structures|Spectrin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of the binding site for inositol phosphates in a PH domain., Hyvonen M, Macias MJ, Nilges M, Oschkinat H, Saraste M, Wilmanns M, EMBO J. 1995 Oct 2;14(19):4676-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7588597 7588597]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Hyvoenen M]]
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[[Category: Hyvoenen, M.]]
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[[Category: Saraste M]]
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[[Category: Saraste, M.]]
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[[Category: Wilmanns M]]
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[[Category: Wilmanns, M.]]
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[[Category: I3P]]
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[[Category: signal transduction protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:54:47 2007''
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STRUCTURE OF THE BINDING SITE FOR INOSITOL PHOSPHATES IN A PH DOMAIN

PDB ID 1btn

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