1fap

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(New page: 200px<br /> <applet load="1fap" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fap, resolution 2.7&Aring;" /> '''THE STRUCTURE OF THE...)
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[[Image:1fap.gif|left|200px]]<br />
 
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<applet load="1fap" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fap, resolution 2.7&Aring;" />
 
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'''THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP'''<br />
 
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==Overview==
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==THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP==
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Rapamycin, a potent immunosuppressive agent, binds two proteins: the, FK506-binding protein (FKBP12) and the FKBP-rapamycin-associated protein, (FRAP). A crystal structure of the ternary complex of human FKBP12, rapamycin, and the FKBP12-rapamycin-binding (FRB) domain of human FRAP at, a resolution of 2.7 angstroms revealed the two proteins bound together as, a result of the ability of rapamycin to occupy two different hydrophobic, binding pockets simultaneously. The structure shows extensive interactions, between rapamycin and both proteins, but fewer interactions between the, proteins. The structure of the FRB domain of FRAP clarifies both, rapamycin-independent and -dependent effects observed for mutants of FRAP, and its homologs in the family of proteins related to the, ataxia-telangiectasia mutant gene product, and it illustrates how a small, cell-permeable molecule can mediate protein dimerization.
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<StructureSection load='1fap' size='340' side='right'caption='[[1fap]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fap]] 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=1FAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAP 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]] 2.7&#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=RAP:RAPAMYCIN+IMMUNOSUPPRESSANT+DRUG'>RAP</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=1fap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fap OCA], [https://pdbe.org/1fap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fap RCSB], [https://www.ebi.ac.uk/pdbsum/1fap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fap ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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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/fa/1fap_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=1fap 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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1FAP 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 RAP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAP OCA].
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*[[FKBP 3D structures|FKBP 3D structures]]
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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==Reference==
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== References ==
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Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP., Choi J, Chen J, Schreiber SL, Clardy J, Science. 1996 Jul 12;273(5272):239-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8662507 8662507]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Chen J]]
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[[Category: Chen, J.]]
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[[Category: Choi J]]
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[[Category: Choi, J.]]
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[[Category: Clardy J]]
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[[Category: Clardy, J.]]
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[[Category: Schreiber SL]]
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[[Category: Schreiber, S.L.]]
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[[Category: RAP]]
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[[Category: complex (isomerase/kinase)]]
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[[Category: fkbp12]]
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[[Category: frap]]
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[[Category: rapamycin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:50:49 2007''
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Current revision

THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP

PDB ID 1fap

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