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New page: left|200px<br /> <applet load="1fkf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fkf, resolution 1.7Å" /> '''ATOMIC STRUCTURE OF ...
 
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[[Image:1fkf.gif|left|200px]]<br />
<applet load="1fkf" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fkf, resolution 1.7&Aring;" />
'''ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX'''<br />


==Overview==
==ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX==
The structure of the human FK506 binding protein (FKBP), complexed with, the immunosuppressant FK506, has been determined to 1.7 angstroms, resolution by x-ray crystallography. The conformation of the protein, changes little upon complexation, but the conformation of FK506 is, markedly different in the bound and unbound forms. The drug's association, with the protein involves five hydrogen bonds, a hydrophobic binding, pocket lined with conserved aromatic residues, and an unusual carbonyl, binding pocket. The nature of this complex has implications for the, mechanism of rotamase catalysis and for the biological actions of FK506, and rapamycin.
<StructureSection load='1fkf' size='340' side='right'caption='[[1fkf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fkf]] 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=1FKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FKF 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</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=1fkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkf OCA], [https://pdbe.org/1fkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fkf RCSB], [https://www.ebi.ac.uk/pdbsum/1fkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fkf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FKB1A_HUMAN FKB1A_HUMAN] Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:9233797</ref> <ref>PMID:16720724</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/fk/1fkf_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=1fkf ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FK5 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FKF OCA].
*[[FKBP 3D structures|FKBP 3D structures]]
 
== References ==
==Reference==
<references/>
Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex., Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J, Science. 1991 May 10;252(5007):839-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1709302 1709302]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Clardy, J.]]
[[Category: Clardy J]]
[[Category: Karplus, P.A.]]
[[Category: Karplus PA]]
[[Category: Schreiber, S.L.]]
[[Category: Schreiber SL]]
[[Category: Standaert, R.F.]]
[[Category: Standaert RF]]
[[Category: Vanduyne, G.D.]]
[[Category: Vanduyne GD]]
[[Category: FK5]]
[[Category: isomerase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:54:08 2007''

Latest revision as of 07:15, 7 February 2024

ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX

1fkf, resolution 1.70Å

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