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[[Image:1c9h.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN==
|PDB= 1c9h |SIZE=350|CAPTION= <scene name='initialview01'>1c9h</scene>, resolution 2.00&Aring;
<StructureSection load='1c9h' size='340' side='right'caption='[[1c9h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=RAP:RAPAMYCIN+IMMUNOSUPPRESSANT+DRUG'>RAP</scene>
<table><tr><td colspan='2'>[[1c9h]] is a 1 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=1C9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9H FirstGlance]. <br>
|ACTIVITY=
</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>
|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RAP:RAPAMYCIN+IMMUNOSUPPRESSANT+DRUG'>RAP</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=1c9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9h OCA], [https://pdbe.org/1c9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9h RCSB], [https://www.ebi.ac.uk/pdbsum/1c9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9h ProSAT]</span></td></tr>
|RELATEDENTRY=[[1fkl|1FKL]], [[1fap|1FAP]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9h OCA], [http://www.ebi.ac.uk/pdbsum/1c9h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c9h RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
== 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/c9/1c9h_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=1c9h ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN'''
==See Also==
 
*[[FKBP 3D structures|FKBP 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
FKBP12.6 is a novel isoform of FKBP12, which selectively binds to the cardiac ryanodine receptor (RyR2). The crystal structure of FKBP12.6 in complex with rapamycin has now been determined at 2.0 A resolution. The structures of FKBP12.6 and FKBP12 are nearly identical, except for a displacement observed in the helical region of FKBP12.6 toward the hydrophobic pocket. This displacement was not predicted by homology modeling studies. Analyses of the residues that are likely to confer the RyR2-binding specificity are presented.
 
==About this Structure==
1C9H is a [[Single protein]] structure of sequence 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=1C9H OCA].
 
==Reference==
Structure of FKBP12.6 in complex with rapamycin., Deivanayagam CC, Carson M, Thotakura A, Narayana SV, Chodavarapu RS, Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):266-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10713512 10713512]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Carson, M.]]
[[Category: Carson M]]
[[Category: Chodavarapu, C S.]]
[[Category: Chodavarapu CS]]
[[Category: Deivanayagam, C C.S.]]
[[Category: Deivanayagam CCS]]
[[Category: Narayana, S V.L.]]
[[Category: Narayana SVL]]
[[Category: Thotakura, A.]]
[[Category: Thotakura A]]
[[Category: complex]]
[[Category: fkbp12]]
[[Category: rapamycin]]
[[Category: ryanodine receptor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:17:18 2008''

Latest revision as of 09:41, 7 February 2024

CRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCINCRYSTAL STRUCTURE OF FKBP12.6 IN COMPLEX WITH RAPAMYCIN

Structural highlights

1c9h is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FKB1B_HUMAN Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1c9h, resolution 2.00Å

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