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==Crystal Structure of Human Tyrosine Hydroxylase Catalytic Domain== | |||
<StructureSection load='2xsn' size='340' side='right' caption='[[2xsn]], [[Resolution|resolution]] 2.68Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xsn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XSN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine_3-monooxygenase Tyrosine 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.2 1.14.16.2] </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=2xsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xsn RCSB], [http://www.ebi.ac.uk/pdbsum/2xsn PDBsum]</span></td></tr> | |||
== | </table> | ||
[[2xsn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSN OCA]. | == Disease == | ||
[[http://www.uniprot.org/uniprot/TY3H_HUMAN TY3H_HUMAN]] Autosomal recessive dopa-responsive dystonia. The disease is caused by mutations affecting the gene represented in this entry. May play a role in the pathogenesis of Parkinson disease (PD). A genome-wide copy number variation analysis has identified a 34 kilobase deletion over the TH gene in a PD patient but not in any controls.<ref>PMID:20809526</ref> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/TY3H_HUMAN TY3H_HUMAN]] Plays an important role in the physiology of adrenergic neurons. | |||
==See Also== | ==See Also== | ||
*[[Tyrosine hydroxylase|Tyrosine hydroxylase]] | *[[Tyrosine hydroxylase|Tyrosine hydroxylase]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Tyrosine 3-monooxygenase]] | [[Category: Tyrosine 3-monooxygenase]] | ||
Revision as of 16:21, 22 October 2014
Crystal Structure of Human Tyrosine Hydroxylase Catalytic DomainCrystal Structure of Human Tyrosine Hydroxylase Catalytic Domain
Structural highlights
Disease[TY3H_HUMAN] Autosomal recessive dopa-responsive dystonia. The disease is caused by mutations affecting the gene represented in this entry. May play a role in the pathogenesis of Parkinson disease (PD). A genome-wide copy number variation analysis has identified a 34 kilobase deletion over the TH gene in a PD patient but not in any controls.[1] Function[TY3H_HUMAN] Plays an important role in the physiology of adrenergic neurons. See AlsoReferences
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