User:Andrea Foote/Sandbox 1: Difference between revisions

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<StructureSection load='5fgp' size='340' side='right' caption='''Drosophila Purα intramolecular domain (purple: PUR repeat I, orange: PUR repeat II) in complex with DNA (green). X-ray diffraction, 2Å resolution ([[5fgp]]).''' scene='78/786627/5fgp_intro/8'>
<StructureSection load='5fgp' size='340' side='right' caption='''Drosophila Purα intramolecular domain (purple: PUR repeat I, orange: PUR repeat II) in complex with DNA (green). X-ray diffraction, 2Å resolution ([[5fgp]]).''' scene='78/786627/5fgp_intro/8'>
== Introduction ==
== Introduction ==
'''Purine-rich element binding protein alpha''' (Purα or PurA) is a transcription factor with a molecular weight of ~35 kDa encoded by the PURA gene. It is known to recognize and bind sequence-specific purine-rich regions of ssDNA and ssRNA. Purα is a member of the PUR family of proteins, including cousins Purβ and two isoforms of Purγ. In its functional dimeric form Purα is known to repress expression of smooth muscle alpha actin (SMαA) and ____. It plays a crucial role in nervous system development, and additionally is known to be involved in cell cycle regulation. Mutations in Purα have been implicated in two neurological diseases: PURA syndrome and Fragile X-associated Tremor/Ataxia Syndrome (FXTAS) (see Disease section).
'''Purine-rich element binding protein alpha''' (Purα or PurA) is a transcription factor with a molecular weight of ~35 kDa encoded by the PURA gene. It is known to bind sequence-specific purine-rich regions of ssDNA and ssRNA, specifically GGN repeats. Purα is a member of the PUR family of proteins, which includes Purβ and two isoforms of Purγ. In its functional dimeric form Purα is known to repress expression of smooth muscle alpha actin (SMαA) encoded by the ''Acta2'' gene. It is also known to be involved in DNA replication and cell cycle regulation as well as mRNA translation. It plays a crucial role in nervous system development, and mutations in Purα have been implicated in two neurological diseases: PURA syndrome and Fragile X-associated Tremor/Ataxia Syndrome (FXTAS) (see Disease section).


== Structure ==
== Structure ==

Revision as of 13:24, 3 May 2018

Purine-rich element binding protein alphaPurine-rich element binding protein alpha

Introduction

Purine-rich element binding protein alpha (Purα or PurA) is a transcription factor with a molecular weight of ~35 kDa encoded by the PURA gene. It is known to bind sequence-specific purine-rich regions of ssDNA and ssRNA, specifically GGN repeats. Purα is a member of the PUR family of proteins, which includes Purβ and two isoforms of Purγ. In its functional dimeric form Purα is known to repress expression of smooth muscle alpha actin (SMαA) encoded by the Acta2 gene. It is also known to be involved in DNA replication and cell cycle regulation as well as mRNA translation. It plays a crucial role in nervous system development, and mutations in Purα have been implicated in two neurological diseases: PURA syndrome and Fragile X-associated Tremor/Ataxia Syndrome (FXTAS) (see Disease section).

Structure

facilitates dimerization of Purα monomers. The association of two repeat III domains forms what is termed the "intermolecular domain".

A PUR domain is analogous to a left-handed handshake. PUR repeat I-II represented from 5fgp.

Function

functions as a homodimer or heterodimer with PurB (and PurG?), PurA is known to repress various genes including

, Y57 (repeat I) and F145 (repeat II) have been implicated in the DNA unwinding activity of PurA.[1]

Disease

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

You may include any references to papers as in: the use of JSmol in Proteopedia [2]


PDB ID 5fgp

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FunctionFunction


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scene='78/786627/5fgp_57and145/1'

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ReferencesReferences

  1. ↑ Weber J, Bao H, Hartlmuller C, Wang Z, Windhager A, Janowski R, Madl T, Jin P, Niessing D. Structural basis of nucleic-acid recognition and double-strand unwinding by the essential neuronal protein Pur-alpha. Elife. 2016 Jan 8;5. pii: e11297. doi: 10.7554/eLife.11297. PMID:26744780 doi:http://dx.doi.org/10.7554/eLife.11297
  2. ↑ 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
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