2rse

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==NMR structure of FKBP12-mTOR FRB domain-rapamycin complex structure determined based on PCS==
==NMR structure of FKBP12-mTOR FRB domain-rapamycin complex structure determined based on PCS==
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<StructureSection load='2rse' size='340' side='right' caption='[[2rse]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2rse' size='340' side='right'caption='[[2rse]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2rse]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSE OCA]. <br>
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<table><tr><td colspan='2'>[[2rse]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSE FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP1A, FKBP1, FKBP12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), MTOR, FRAP, FRAP1, FRAP2, RAFT1, RAPT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2rse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rse OCA], [https://pdbe.org/2rse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rse RCSB], [https://www.ebi.ac.uk/pdbsum/2rse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rse ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rse OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rse RCSB], [http://www.ebi.ac.uk/pdbsum/2rse PDBsum]</span></td></tr>
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== Function ==
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<table>
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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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.,Kobashigawa Y, Saio T, Ushio M, Sekiguchi M, Yokochi M, Ogura K, Inagaki F J Biomol NMR. 2012 May;53(1):53-63. Epub 2012 Apr 10. PMID:22487935<ref>PMID:22487935</ref>
Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.,Kobashigawa Y, Saio T, Ushio M, Sekiguchi M, Yokochi M, Ogura K, Inagaki F J Biomol NMR. 2012 May;53(1):53-63. Epub 2012 Apr 10. PMID:22487935<ref>PMID:22487935</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2rse" style="background-color:#fffaf0;"></div>
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==See Also==
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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]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</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: Inagaki, F.]]
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[[Category: Inagaki F]]
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[[Category: Kobashigawa, Y.]]
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[[Category: Kobashigawa Y]]
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[[Category: Saio, T.]]
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[[Category: Saio T]]
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[[Category: Ushio, M.]]
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[[Category: Ushio M]]
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[[Category: Fk506]]
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[[Category: Fkbp12]]
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[[Category: Isomerase-transferase complex]]
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[[Category: Lanthanide]]
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[[Category: Pc]]
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[[Category: Rapamycin]]
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Current revision

NMR structure of FKBP12-mTOR FRB domain-rapamycin complex structure determined based on PCS

PDB ID 2rse

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