1fkr: Difference between revisions
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<StructureSection load='1fkr' size='340' side='right'caption='[[1fkr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1fkr' size='340' side='right'caption='[[1fkr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fkr]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1fkr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FKR FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fks|1fks]], [[1fkt|1fkt]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fks|1fks]], [[1fkt|1fkt]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkr OCA], [https://pdbe.org/1fkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fkr RCSB], [https://www.ebi.ac.uk/pdbsum/1fkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fkr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[ | *[[FKBP 3D structures|FKBP 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
