4c02
From Proteopedia
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| - | + | ==Crystal structure of human ACVR1 (ALK2) in complex with FKBP12.6 and dorsomorphin== | |
| - | + | <StructureSection load='4c02' size='340' side='right' caption='[[4c02]], [[Resolution|resolution]] 2.17Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | ==Disease== | + | <table><tr><td colspan='2'>[[4c02]] is a 2 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=4C02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C02 FirstGlance]. <br> |
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=TAK:6-[4-(2-PIPERIDIN-1-YLETHOXY)PHENYL]-3-PYRIDIN-4-YLPYRAZOLO[1,5-A]PYRIMIDINE'>TAK</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <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=4c02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c02 RCSB], [http://www.ebi.ac.uk/pdbsum/4c02 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
[[http://www.uniprot.org/uniprot/ACVR1_HUMAN ACVR1_HUMAN]] Fibrodysplasia ossificans progressiva. Defects in ACVR1 are a cause of fibrodysplasia ossificans progressiva (FOP) [MIM:[http://omim.org/entry/135100 135100]]. FOP is a rare autosomal dominant disorder of skeletal malformations and progressive extraskeletal ossification. Heterotopic ossification in FOP begins in childhood and can be induced by trauma or may occur without warning. Bone formation is episodic and progressive, leading to extra-articular ankylosis of all major joints of the axial and appendicular skeleton, rendering movement impossible.<ref>PMID:16642017</ref> <ref>PMID:19085907</ref> <ref>PMID:19330033</ref> | [[http://www.uniprot.org/uniprot/ACVR1_HUMAN ACVR1_HUMAN]] Fibrodysplasia ossificans progressiva. Defects in ACVR1 are a cause of fibrodysplasia ossificans progressiva (FOP) [MIM:[http://omim.org/entry/135100 135100]]. FOP is a rare autosomal dominant disorder of skeletal malformations and progressive extraskeletal ossification. Heterotopic ossification in FOP begins in childhood and can be induced by trauma or may occur without warning. Bone formation is episodic and progressive, leading to extra-articular ankylosis of all major joints of the axial and appendicular skeleton, rendering movement impossible.<ref>PMID:16642017</ref> <ref>PMID:19085907</ref> <ref>PMID:19330033</ref> | ||
| - | + | == Function == | |
| - | ==Function== | + | |
[[http://www.uniprot.org/uniprot/ACVR1_HUMAN ACVR1_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 activin. May be involved for left-right pattern formation during embryogenesis (By similarity). [[http://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN]] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | [[http://www.uniprot.org/uniprot/ACVR1_HUMAN ACVR1_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 activin. May be involved for left-right pattern formation during embryogenesis (By similarity). [[http://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN]] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[FK506 binding protein|FK506 binding protein]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | <references | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Human]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
| - | + | [[Category: Arrowsmith, C H]] | |
| - | [[Category: Arrowsmith, C H | + | [[Category: Bountra, C]] |
| - | [[Category: Bountra, C | + | [[Category: Bradley, A]] |
| - | [[Category: Bradley, A | + | [[Category: Bullock, A]] |
| - | [[Category: Bullock, A | + | [[Category: Delft, F von]] |
| - | [[Category: Delft, F von | + | [[Category: Edwards, A M]] |
| - | [[Category: Edwards, A M | + | [[Category: Krojer, T]] |
| - | [[Category: Krojer, T | + | [[Category: Kupinska, K]] |
| - | [[Category: Kupinska, K | + | [[Category: Riesebos, E]] |
| - | [[Category: Riesebos, E | + | [[Category: Shrestha, L]] |
| - | [[Category: Shrestha, L | + | [[Category: Vollmar, M]] |
| - | [[Category: Vollmar, M | + | [[Category: Williams, E]] |
| - | [[Category: Williams, E | + | |
[[Category: Dorsomorphin]] | [[Category: Dorsomorphin]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Transferase-isomerase complex]] | [[Category: Transferase-isomerase complex]] | ||
Revision as of 07:49, 26 March 2015
Crystal structure of human ACVR1 (ALK2) in complex with FKBP12.6 and dorsomorphin
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