1aui: Difference between revisions

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New page: left|200px<br /> <applet load="1aui" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aui, resolution 2.1Å" /> '''HUMAN CALCINEURIN HE...
 
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[[Image:1aui.gif|left|200px]]<br />
<applet load="1aui" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1aui, resolution 2.1&Aring;" />
'''HUMAN CALCINEURIN HETERODIMER'''<br />


==Overview==
==HUMAN CALCINEURIN HETERODIMER==
Calcineurin (CaN) is a calcium- and calmodulin-dependent protein, serine/threonine phosphate which is critical for several important, cellular processes, including T-cell activation. CaN is the target of the, immunosuppressive drugs cyclosporin A and FK506, which inhibit CaN after, forming complexes with cytoplasmic binding proteins (cyclophilin and, FKBP12, respectively). We report here the crystal structures of, full-length human CaN at 2.1 A resolution and of the complex of human CaN, with FKBP12-FK506 at 3.5 A resolution. In the native CaN structure, an, auto-inhibitory element binds at the Zn/Fe-containing active site. The, metal-site geometry and active-site water structure suggest a catalytic, mechanism involving nucleophilic attack on the substrate phosphate by a, metal-activated ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8524402 (full description)]]
<StructureSection load='1aui' size='340' side='right'caption='[[1aui]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1aui]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aui OCA], [https://pdbe.org/1aui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aui RCSB], [https://www.ebi.ac.uk/pdbsum/1aui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aui ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref> <ref>PMID:18838687</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1aui_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1aui ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AUI is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA, ZN and FE as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUI OCA]].
*[[Calcineurin|Calcineurin]]
 
*[[Calcineurin 3D structures|Calcineurin 3D structures]]
==Reference==
== References ==
Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex., Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al., Nature. 1995 Dec 7;378(6557):641-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8524402 8524402]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Kissinger, C.R.]]
[[Category: Kissinger CR]]
[[Category: Knighton, D.R.]]
[[Category: Knighton DR]]
[[Category: Lewis, C.T.]]
[[Category: Lewis CT]]
[[Category: Parge, H.E.]]
[[Category: Parge HE]]
[[Category: Pelletier, L.A.]]
[[Category: Pelletier LA]]
[[Category: Tempczyk, A.]]
[[Category: Tempczyk A]]
[[Category: Villafranca, J.E.]]
[[Category: Villafranca JE]]
[[Category: CA]]
[[Category: FE]]
[[Category: ZN]]
[[Category: hydrolase]]
[[Category: immunosuppression]]
[[Category: phosphatase]]
 
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Latest revision as of 06:33, 7 February 2024

HUMAN CALCINEURIN HETERODIMER

1aui, resolution 2.10Å

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