Sandbox Reserved 1694
From Proteopedia
(Difference between revisions)
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These <scene name='89/892737/Amino_acids_rotating/3'>amino acids</scene> play an extensive role in interactions between 1-PO4 and 2-PO4 of the substrate to the active site. Also, there are a few different amino acids (<scene name='89/892737/Amino_acids_for_ring/1'>amino acids</scene>) that interact with the inositol ring and help reinforce the binding of the Ins(1,4)P2. | These <scene name='89/892737/Amino_acids_rotating/3'>amino acids</scene> play an extensive role in interactions between 1-PO4 and 2-PO4 of the substrate to the active site. Also, there are a few different amino acids (<scene name='89/892737/Amino_acids_for_ring/1'>amino acids</scene>) that interact with the inositol ring and help reinforce the binding of the Ins(1,4)P2. | ||
- | <ref>PMID:33172890</ref> | + | <ref name="dollins">PMID:33172890</ref> |
== Structural highlights == | == Structural highlights == | ||
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== Other important features == | == Other important features == | ||
- | In the structure INPP1D54A, there is a mutation in the amino acid aspartic acid (D)54 and causes it to change to alanine (A)54 (<scene name='89/892737/Alanine/1'>mutation in D54</scene>). This mutation does not impact the substrate affinity but does decrease the activity of INPP1. <ref | + | In the structure INPP1D54A, there is a mutation in the amino acid aspartic acid (D)54 and causes it to change to alanine (A)54 (<scene name='89/892737/Alanine/1'>mutation in D54</scene>). This mutation does not impact the substrate affinity but does decrease the activity of INPP1. <ref name="dollins" /> |
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
- | <references/> | + | <references /> |
Revision as of 19:47, 7 November 2021
This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699. |
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References
- ↑ 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
- ↑ 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
- ↑ 3.0 3.1 Dollins DE, Xiong JP, Endo-Streeter S, Anderson DE, Bansal VS, Ponder JW, Ren Y, York JD. A Structural Basis for Lithium and Substrate Binding of an Inositide Phosphatase. J Biol Chem. 2020 Nov 10. pii: RA120.014057. doi: 10.1074/jbc.RA120.014057. PMID:33172890 doi:http://dx.doi.org/10.1074/jbc.RA120.014057