3dl9: Difference between revisions
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==Crystal structure of CYP2R1 in complex with 1-alpha-hydroxy-vitamin D2== | ==Crystal structure of CYP2R1 in complex with 1-alpha-hydroxy-vitamin D2== | ||
<StructureSection load='3dl9' size='340' side='right' caption='[[3dl9]], [[Resolution|resolution]] 2.72Å' scene=''> | <StructureSection load='3dl9' size='340' side='right'caption='[[3dl9]], [[Resolution|resolution]] 2.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3dl9]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3dl9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DL9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=V2H:(1S,3R,5Z,7E,22E)-9,10-SECOERGOSTA-5,7,10,22-TETRAENE-1,3-DIOL'>V2H</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3czh|3czh]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3czh|3czh]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP2R1 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP2R1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3dl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl9 OCA], [https://pdbe.org/3dl9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dl9 RCSB], [https://www.ebi.ac.uk/pdbsum/3dl9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dl9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[[ | [[https://www.uniprot.org/uniprot/CP2R1_HUMAN CP2R1_HUMAN]] Defects in CYP2R1 are the cause of rickets vitamin D-dependent type 1B (VDDR1B) [MIM:[https://omim.org/entry/600081 600081]]; also known as pseudovitamin D(3) deficiency rickets due to 25-hydroxylase deficiency. A disorder caused by a selective deficiency of the active form of vitamin D (1,25-dihydroxyvitamin D3) and resulting in defective bone mineralization and clinical features of rickets. The patients sera have low calcium concentrations, low phosphate concentrations, elevated alkaline phosphatase activityand low levels of 25-hydroxyvitamin D.<ref>PMID:15128933</ref> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CP2R1_HUMAN CP2R1_HUMAN]] Has a D-25-hydroxylase activity on both forms of vitamin D, vitamin D(2) and D(3).<ref>PMID:12867411</ref> <ref>PMID:15465040</ref> <ref>PMID:18511070</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/3dl9_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/3dl9_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dl9 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dl9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | |||
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bochkarev, A]] | [[Category: Bochkarev, A]] |
Revision as of 11:01, 9 February 2022
Crystal structure of CYP2R1 in complex with 1-alpha-hydroxy-vitamin D2Crystal structure of CYP2R1 in complex with 1-alpha-hydroxy-vitamin D2
Structural highlights
Disease[CP2R1_HUMAN] Defects in CYP2R1 are the cause of rickets vitamin D-dependent type 1B (VDDR1B) [MIM:600081]; also known as pseudovitamin D(3) deficiency rickets due to 25-hydroxylase deficiency. A disorder caused by a selective deficiency of the active form of vitamin D (1,25-dihydroxyvitamin D3) and resulting in defective bone mineralization and clinical features of rickets. The patients sera have low calcium concentrations, low phosphate concentrations, elevated alkaline phosphatase activityand low levels of 25-hydroxyvitamin D.[1] Function[CP2R1_HUMAN] Has a D-25-hydroxylase activity on both forms of vitamin D, vitamin D(2) and D(3).[2] [3] [4] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Large Structures
- Arrowsmith, C H
- Bochkarev, A
- Bountra, C
- Edwards, A M
- Gilep, A A
- Loppnau, P
- Park, H
- Structural genomic
- Strushkevich, N V
- Tempel, W
- Wilkstrom, M
- Cytochrome p450
- Disease mutation
- Drug metabolism
- Endoplasmic reticulum
- Heme
- Iron
- Membrane
- Metal-binding
- Microsome
- Monooxygenase
- Oxidoreductase
- Sgc
- Vitamin d
- Vitamin s 25-hydroxylase