4zel: Difference between revisions
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The entry | ==Human dopamine beta-hydroxylase== | ||
<StructureSection load='4zel' size='340' side='right'caption='[[4zel]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zel]] is a 2 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=4ZEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZEL FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zel OCA], [https://pdbe.org/4zel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zel RCSB], [https://www.ebi.ac.uk/pdbsum/4zel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zel ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/DOPO_HUMAN DOPO_HUMAN] Dopamine beta-hydroxylase deficiency. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DOPO_HUMAN DOPO_HUMAN] Conversion of dopamine to noradrenaline. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The norepinephrine pathway is believed to modulate behavioral and physiological processes, such as mood, overall arousal, and attention. Furthermore, abnormalities in the pathway have been linked to numerous diseases, for example hypertension, depression, anxiety, Parkinson's disease, schizophrenia, Alzheimer's disease, attention deficit hyperactivity disorder, and cocaine dependence. We report the crystal structure of human dopamine beta-hydroxylase, which is the enzyme converting dopamine to norepinephrine. The structure of the DOMON (dopamine beta-monooxygenase N-terminal) domain, also found in >1600 other proteins, reveals a possible metal-binding site and a ligand-binding pocket. The catalytic core structure shows two different conformations: an open active site, as also seen in another member of this enzyme family [the peptidylglycine alpha-hydroxylating (and alpha-amidating) monooxygenase], and a closed active site structure, in which the two copper-binding sites are only 4 to 5 A apart, in what might be a coupled binuclear copper site. The dimerization domain adopts a conformation that bears no resemblance to any other known protein structure. The structure provides new molecular insights into the numerous devastating disorders of both physiological and neurological origins associated with the dopamine system. | |||
The crystal structure of human dopamine beta-hydroxylase at 2.9 A resolution.,Vendelboe TV, Harris P, Zhao Y, Walter TS, Harlos K, El Omari K, Christensen HE Sci Adv. 2016 Apr 8;2(4):e1500980. doi: 10.1126/sciadv.1500980. eCollection 2016 , Apr. PMID:27152332<ref>PMID:27152332</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4zel" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Hydroxylases 3D structures|Hydroxylases 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Christensen HEM]] | |||
[[Category: Harlos K]] | |||
[[Category: Harris P]] | |||
[[Category: Omari K]] | |||
[[Category: Vendelboe TV]] | |||
[[Category: Walter T]] | |||
[[Category: Zhao Y]] | |||
Latest revision as of 11:34, 9 October 2024
Human dopamine beta-hydroxylaseHuman dopamine beta-hydroxylase
Structural highlights
DiseaseDOPO_HUMAN Dopamine beta-hydroxylase deficiency. The disease is caused by mutations affecting the gene represented in this entry. FunctionDOPO_HUMAN Conversion of dopamine to noradrenaline. Publication Abstract from PubMedThe norepinephrine pathway is believed to modulate behavioral and physiological processes, such as mood, overall arousal, and attention. Furthermore, abnormalities in the pathway have been linked to numerous diseases, for example hypertension, depression, anxiety, Parkinson's disease, schizophrenia, Alzheimer's disease, attention deficit hyperactivity disorder, and cocaine dependence. We report the crystal structure of human dopamine beta-hydroxylase, which is the enzyme converting dopamine to norepinephrine. The structure of the DOMON (dopamine beta-monooxygenase N-terminal) domain, also found in >1600 other proteins, reveals a possible metal-binding site and a ligand-binding pocket. The catalytic core structure shows two different conformations: an open active site, as also seen in another member of this enzyme family [the peptidylglycine alpha-hydroxylating (and alpha-amidating) monooxygenase], and a closed active site structure, in which the two copper-binding sites are only 4 to 5 A apart, in what might be a coupled binuclear copper site. The dimerization domain adopts a conformation that bears no resemblance to any other known protein structure. The structure provides new molecular insights into the numerous devastating disorders of both physiological and neurological origins associated with the dopamine system. The crystal structure of human dopamine beta-hydroxylase at 2.9 A resolution.,Vendelboe TV, Harris P, Zhao Y, Walter TS, Harlos K, El Omari K, Christensen HE Sci Adv. 2016 Apr 8;2(4):e1500980. doi: 10.1126/sciadv.1500980. eCollection 2016 , Apr. PMID:27152332[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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