This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Tom almog/UCP1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:01, 23 November 2014) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
==Your Heading Here (maybe something like 'Structure')==
==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene='60/607861/Ucp1/1'>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene='60/607861/Ucp1/1'>
-
This is a default text for your page '''Tom almog/test page'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
+
The uncoupling protein UCP1 is a member of a superfamily of homologous proteins formed by the mitochondrial metabolite transporters.
-
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
+
-
 
+
-
The uncoupling protein UCP1 is a member of a superfamily of homologous proteins formed by the
+
-
mitochondrial metabolite transporters.
+
== Function ==
== Function ==
Line 13: Line 9:
== Disease ==
== Disease ==
 +
 +
Knockout of the UCP1 gene produces mice that are cold intolerant.
== Relevance ==
== Relevance ==
Line 21: Line 19:
UCP1 is composed of three repeated domains of approximately 100 amino acids each.
UCP1 is composed of three repeated domains of approximately 100 amino acids each.
-
The nucleotide binding site is specific for purine nucleotides and tolerates a number of derivatives. The strong pH dependency facilitates regulation of nucleotide binding and thus H+ translocation.
+
Its activity is regulated by purine nucleotides (inhibitors) and non-esterified fatty acids (activators).
It proposes that in the protein core there must exist a hydrophilic translocation pore whose access is controlled by gates. It is highly likely that the hydrophilic channel is formed by the transmembrane á-helices and that loops contribute to the formation of the gates.
It proposes that in the protein core there must exist a hydrophilic translocation pore whose access is controlled by gates. It is highly likely that the hydrophilic channel is formed by the transmembrane á-helices and that loops contribute to the formation of the gates.
-
<scene name='60/607861/Ucp1/1'>UCP1</scene>
+
<scene name='60/607861/Ucp1_active_site/5'>UCP1's active site</scene>
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Current revision

Your Heading Here (maybe something like 'Structure')

Caption for this structure

Drag the structure with the mouse to rotate

References

Proteopedia Page Contributors and Editors (what is this?)

Tom Almog

Retrieved from "http://52.214.119.220/wiki/index.php/Tom_almog/UCP1"
Personal tools