Sandbox Reserved 1585

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==Human Carbonic Anhydrase 1==
==Human Carbonic Anhydrase 1==
<StructureSection load='2cab' size='340' side='right' caption='Human Carbonic Anhydrase' scene=''>
<StructureSection load='2cab' size='340' side='right' caption='Human Carbonic Anhydrase' scene=''>
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol <ref name="ref1">PMID:6430186</ref> to the rescue. <ref>DOI 10.1002/ijch.201300024</ref>
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== Overview ==
== Overview ==
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Test text<ref name="ref1" />
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Human carbonic anhydrase are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. This protein contains a zinc ion and 260 amino acid residues. Human carbonic anhydrase activation has been associated with cardiomyopathy in diabetics.<ref name="ref2">PMID:24670789</ref> In diabetic patents with postinfarct heart failure it was found that their level of human carbonic anhyrase 1 was significantly higher then the levels of non-diabetics.<ref name="ref2" /> Developing an inhibitor for human carbonic anhydrase 1 is contributing to the treatment of these diseases.<ref>DOI 10.1038/nrd2467</ref>
Human carbonic anhydrase are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. This protein contains a zinc ion and 260 amino acid residues. Human carbonic anhydrase activation has been associated with cardiomyopathy in diabetics.<ref name="ref2">PMID:24670789</ref> In diabetic patents with postinfarct heart failure it was found that their level of human carbonic anhyrase 1 was significantly higher then the levels of non-diabetics.<ref name="ref2" /> Developing an inhibitor for human carbonic anhydrase 1 is contributing to the treatment of these diseases.<ref>DOI 10.1038/nrd2467</ref>
== Function ==
== Function ==
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This protein participates in biological processes like cellular respiration, calcification, pH balance and bone resorption. It also participates in the formation of cerebrospinal fluid, saliva and gastic acid.
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Human carbonic anhydrase 1 is found in cytosol of red blood cells, GI tract and cardiac tissue.<ref name="ref3">PMID:6430186</ref> It participates in biological processes like cellular respiration, calcification, pH balance and bone resorption.<ref name="ref3" /> It also participates in the formation of cerebrospinal fluid, saliva and gastic acid.<ref name="ref3" />
== Structural highlights ==
== Structural highlights ==
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A predominant structural are the <scene name='82/824630/Hca1_sheets/1'>twisted β-pleated sheets</scene>.<ref name="ref1" /> An important feature of the <scene name='82/824630/Hca1_helix/1'>α-helices</scene> is that they are <scene name='82/824630/Hca1_hydrogenbond/1'>hydrogen bonds absent</scene> that had previously been expected to exist.<ref name="ref1" />
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A predominant structural are the <scene name='82/824630/Hca1_sheets/1'>twisted β-pleated sheets</scene>.<ref name="ref1">PMID:6430186</ref> An important feature of the <scene name='82/824630/Hca1_helix/1'>α-helices</scene> is that they are <scene name='82/824630/Hca1_hydrogenbond/1'>hydrogen bonds absent</scene> that had previously been expected to exist.<ref name="ref1" />
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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.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Current revision

This Sandbox is Reserved from September 14, 2021, through May 31, 2022, for use in the class Introduction to Biochemistry taught by User:John Means at the University of Rio Grande, Rio Grande, OH, USA. This reservation includes 5 reserved sandboxes (Sandbox Reserved 1590 through Sandbox Reserved 1594).
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
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More help: Help:Editing. For an example of a student Proteopedia page, please see Photosystem II, Tetanospasmin, or Guanine riboswitch.

Human Carbonic Anhydrase 1

Human Carbonic Anhydrase

Drag the structure with the mouse to rotate

References

  1. ↑ 1.0 1.1 Torella D, Ellison GM, Torella M, Vicinanza C, Aquila I, Iaconetti C, Scalise M, Marino F, Henning BJ, Lewis FC, Gareri C, Lascar N, Cuda G, Salvatore T, Nappi G, Indolfi C, Torella R, Cozzolino D, Sasso FC. Carbonic anhydrase activation is associated with worsened pathological remodeling in human ischemic diabetic cardiomyopathy. J Am Heart Assoc. 2014 Mar 26;3(2):e000434. doi: 10.1161/JAHA.113.000434. PMID:24670789 doi:http://dx.doi.org/10.1161/JAHA.113.000434
  2. ↑ Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov. 2008 Feb;7(2):168-81. doi: 10.1038/nrd2467. PMID:18167490 doi:http://dx.doi.org/10.1038/nrd2467
  3. ↑ 3.0 3.1 3.2 Kannan KK, Ramanadham M, Jones TA. Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I. Ann N Y Acad Sci. 1984;429:49-60. PMID:6430186
  4. ↑ 4.0 4.1 Kannan KK, Ramanadham M, Jones TA. Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I. Ann N Y Acad Sci. 1984;429:49-60. PMID:6430186
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