1aui: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1aui.jpg|left|200px]]


{{Structure
==HUMAN CALCINEURIN HETERODIMER==
|PDB= 1aui |SIZE=350|CAPTION= <scene name='initialview01'>1aui</scene>, resolution 2.1&Aring;
<StructureSection load='1aui' size='340' side='right'caption='[[1aui]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE= <scene name='pdbsite=CA1:Ca+Binding+Site'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Binding+Site'>CA2</scene>, <scene name='pdbsite=CA3:Ca+Binding+Site'>CA3</scene>, <scene name='pdbsite=CA4:Ca+Binding+Site'>CA4</scene>, <scene name='pdbsite=FEB:Fe+Binding+Site'>FEB</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site'>ZNB</scene>
== Structural highlights ==
|LIGAND= <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>
<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>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span>
</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>
|GENE=
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aui OCA], [http://www.ebi.ac.uk/pdbsum/1aui PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aui RCSB]</span>
== 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>


'''HUMAN CALCINEURIN HETERODIMER'''
==See Also==
 
*[[Calcineurin|Calcineurin]]
 
*[[Calcineurin 3D structures|Calcineurin 3D structures]]
==Overview==
== References ==
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 water molecule. In the FKBP12-FK506-CaN complex, the auto-inhibitory element is displaced from the active site. The site of binding of FKBP12-FK506 appears to be shared by other non-competitive inhibitors of calcineurin, including a natural anchoring protein.
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
1AUI is a [[Protein complex]] structure of sequences from [http://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].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/8524402 8524402]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Kissinger CR]]
[[Category: Kissinger, C R.]]
[[Category: Knighton DR]]
[[Category: Knighton, D R.]]
[[Category: Lewis CT]]
[[Category: Lewis, C T.]]
[[Category: Parge HE]]
[[Category: Parge, H E.]]
[[Category: Pelletier LA]]
[[Category: Pelletier, L A.]]
[[Category: Tempczyk A]]
[[Category: Tempczyk, A.]]
[[Category: Villafranca JE]]
[[Category: Villafranca, J E.]]
[[Category: hydrolase]]
[[Category: immunosuppression]]
[[Category: phosphatase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:47:50 2008''

Latest revision as of 06:33, 7 February 2024

HUMAN CALCINEURIN HETERODIMER

1aui, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA