3s5d: Difference between revisions

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~~[[Image:3s5d.png|left|200px]]~~

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===Crystal structure of human frataxin variant W155A===

==Disease==

[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Defects in FXN are the cause of Friedreich ataxia (FRDA) [MIM:[http://omim.org/entry/229300 229300]]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.[:][:]<ref>PMID:9150176</ref><ref>PMID:9779809</ref><ref>PMID:10732799</ref><ref>PMID:9989622</ref>[:]<ref>PMID:10874325</ref><ref>PMID:19629184</ref>

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==Function==

~~The line below this paragraph, {{ABSTRACT_PUBMED_21671584}}, adds the Publication Abstract to the page~~

[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.<ref>PMID:20053667</ref><ref>PMID:11823441</ref><ref>PMID:12755598</ref><ref>PMID:12785837</ref><ref>PMID:15123683</ref><ref>PMID:15247478</ref><ref>PMID:15641778</ref><ref>PMID:16239244</ref><ref>PMID:16608849</ref>

~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~), ~~where 21671584~~ is the ~~PubMed ID number~~.

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~~{{ABSTRACT_PUBMED_21671584}}~~

==About this Structure==

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==Reference==

[[Category: Ferroxidase]]

[[Category: Homo sapiens]]

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@@ Line 1: / Line 1: @@
-[[Image:3s5d.png|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_3s5d", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
 {{STRUCTURE_3s5d|  PDB=3s5d  |  SCENE=  }}
 ===Crystal structure of human frataxin variant W155A===
+{{ABSTRACT_PUBMED_21671584}}
+==Disease==
+[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Defects in FXN are the cause of Friedreich ataxia (FRDA) [MIM:[http://omim.org/entry/229300 229300]]. FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region.[:][:]<ref>PMID:9150176</ref><ref>PMID:9779809</ref><ref>PMID:10732799</ref><ref>PMID:9989622</ref>[:]<ref>PMID:10874325</ref><ref>PMID:19629184</ref>
-<!--
+==Function==
-The line below this paragraph, {{ABSTRACT_PUBMED_21671584}}, adds the Publication Abstract to the page
+[[http://www.uniprot.org/uniprot/FRDA_HUMAN FRDA_HUMAN]] Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1.<ref>PMID:20053667</ref><ref>PMID:11823441</ref><ref>PMID:12755598</ref><ref>PMID:12785837</ref><ref>PMID:15123683</ref><ref>PMID:15247478</ref><ref>PMID:15641778</ref><ref>PMID:16239244</ref><ref>PMID:16608849</ref>
-(as it appears on PubMed at http://www.pubmed.gov), where 21671584 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_21671584}}
 ==About this Structure==
@@ Line 22: / Line 13: @@
 ==Reference==
-<ref group="xtra">PMID:021671584</ref><references group="xtra"/>
+<ref group="xtra">PMID:021671584</ref><references group="xtra"/><references/>
 [[Category: Ferroxidase]]
 [[Category: Homo sapiens]]