5i7q
From Proteopedia
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<StructureSection load='5i7q' size='340' side='right'caption='[[5i7q]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5i7q' size='340' side='right'caption='[[5i7q]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5i7q]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5i7q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I7Q FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=5i7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i7q OCA], [https://pdbe.org/5i7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i7q RCSB], [https://www.ebi.ac.uk/pdbsum/5i7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i7q ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [https://www.uniprot.org/uniprot/FKBX_ECOLI FKBX_ECOLI] PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln.[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> |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dobbek | + | [[Category: Dobbek H]] |
| - | [[Category: Jakob | + | [[Category: Jakob RP]] |
| - | [[Category: Schmid | + | [[Category: Schmid FX]] |
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Current revision
Crystal structure of Fkbp12-IF(SlpA), a chimeric protein of human Fkbp12 and the insert in flap domain of Ecoli SlpA
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