Sandbox Reserved 1326

From Proteopedia

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Protein binding:Selectively binds to other protein complexes non-covalently. 1a4y also works to inhibit ANG in order to inhibit angiogenesis, along with RNASE1 to inhibit an endonuclease that cleaves phosphodiester bonds, and RNASE2 .
Protein binding:Selectively binds to other protein complexes non-covalently. 1a4y also works to inhibit ANG in order to inhibit angiogenesis, along with RNASE1 to inhibit an endonuclease that cleaves phosphodiester bonds, and RNASE2 .
== Disease ==
== Disease ==
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Ang has a role in cancers and tumor growth. A mutation in 1a4y which results in decreased activity and thus increased activity of Ang could lead to tumor growth.
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Ang has a role in cancers and tumor growth. A mutation in 1a4y which results in decreased activity and thus increased activity of Ang could lead to tumor growth. Ang has also been theorized as a protector of the central nervous system and thus over-production of 1a4y may result in limited Ang and thus neurodegenerative diseases.
== Relevance ==
== Relevance ==

Revision as of 21:40, 20 February 2018

This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430.
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  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
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Structure of la4y

Ribonuclease Inhibitor-Angiogenin Complex

Drag the structure with the mouse to rotate


</StructureSection>

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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