3mdy

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==Crystal structure of the cytoplasmic domain of the bone morphogenetic protein receptor type-1B (BMPR1B) in complex with FKBP12 and LDN-193189==
==Crystal structure of the cytoplasmic domain of the bone morphogenetic protein receptor type-1B (BMPR1B) in complex with FKBP12 and LDN-193189==
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<StructureSection load='3mdy' size='340' side='right' caption='[[3mdy]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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<StructureSection load='3mdy' size='340' side='right'caption='[[3mdy]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3mdy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MDY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3mdy]] is a 4 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=3MDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MDY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LDN:4-[6-(4-PIPERAZIN-1-YLPHENYL)PYRAZOLO[1,5-A]PYRIMIDIN-3-YL]QUINOLINE'>LDN</scene></td></tr>
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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]] 2.05&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMPR1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), FKBP12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=LDN:4-[6-(4-PIPERAZIN-1-YLPHENYL)PYRAZOLO[1,5-A]PYRIMIDIN-3-YL]QUINOLINE'>LDN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein_serine/threonine_kinase Receptor protein serine/threonine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.30 2.7.11.30] </span></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=3mdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mdy OCA], [https://pdbe.org/3mdy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mdy RCSB], [https://www.ebi.ac.uk/pdbsum/3mdy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mdy ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mdy OCA], [http://pdbe.org/3mdy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mdy RCSB], [http://www.ebi.ac.uk/pdbsum/3mdy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mdy ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/BMR1B_HUMAN BMR1B_HUMAN]] Brachydactyly type A2;Brachydactyly type C;Acromesomelic dysplasia, Grebe type. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/BMR1B_HUMAN BMR1B_HUMAN] Brachydactyly type A2;Brachydactyly type C;Acromesomelic dysplasia, Grebe type. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BMR1B_HUMAN BMR1B_HUMAN]] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5. [[http://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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[https://www.uniprot.org/uniprot/BMR1B_HUMAN BMR1B_HUMAN] On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.
== 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==
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*[[FK506 binding protein|FK506 binding protein]]
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*[[FKBP 3D structures|FKBP 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Receptor protein serine/threonine kinase]]
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[[Category: Large Structures]]
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[[Category: Alfano, I]]
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[[Category: Alfano I]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Bullock, A]]
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[[Category: Bullock A]]
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[[Category: Chaikuad, A]]
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[[Category: Chaikuad A]]
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[[Category: Cooper, C]]
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[[Category: Cooper C]]
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[[Category: Daga, N]]
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[[Category: Daga N]]
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[[Category: Delft, F von]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Knapp S]]
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[[Category: Knapp, S]]
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[[Category: Krojer T]]
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[[Category: Krojer, T]]
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[[Category: Mahajan P]]
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[[Category: Mahajan, P]]
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[[Category: Sanvitale C]]
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[[Category: Structural genomic]]
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[[Category: Weigelt J]]
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[[Category: Sanvitale, C]]
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[[Category: Von Delft F]]
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[[Category: Weigelt, J]]
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[[Category: Atp-binding]]
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[[Category: Disease mutation]]
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[[Category: Kinase]]
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[[Category: Receptor serine/threonine kinase]]
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[[Category: Rotamase]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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[[Category: Transferase-isomerase complex]]
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Current revision

Crystal structure of the cytoplasmic domain of the bone morphogenetic protein receptor type-1B (BMPR1B) in complex with FKBP12 and LDN-193189

PDB ID 3mdy

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