JMS/Sandbox/msn2 1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
<StructureSection size='340' side='right' caption='Caption for this structure' scene=''>
+
<StructureSection size='340' side='right' caption='Caption for this structure' scene='10/1080617/Msn2/1'>
-
<scene name='10/1080617/Msn2/1'>TextToBeDisplayed</scene>
+
<scene name='10/1080617/Msn2/1'>initial view</scene>
</StructureSection>
</StructureSection>

Revision as of 13:33, 11 May 2025

Caption for this structure

Drag the structure with the mouse to rotate

The 3D structure shown is a predicted model from AlphaFold, providing insights into Msn2’s fold, as no experimental structures are currently available. The model is based on the 704-amino-acid sequence from [UniProt: P33748](https://www.uniprot.org/uniprotkb/P33748/entry).

Contents

Interactive Molecular Tour

Explore Msn2’s structural features using the buttons below, powered by JSmol scripts adapted from the [JSmol documentation](https://chemapps.stolaf.edu/jmol/docs/):

Zinc Finger Domains

Msn2 has two C2H2 zinc finger domains at residues 649–670 and 676–698, critical for binding STREs (5'-CCCCT-3') in DNA ([SGD: MSN2](https://www.yeastgenome.org/locus/S000004640)). These domains, identified in the sequence (NP_013751.1), coordinate zinc ions via cysteine and histidine residues, stabilizing the DNA-binding motif.

Phosphorylation Sites

Msn2 is phosphorylated on 22 residues, with six key sites regulated by PKA: S288, S582, S620, S625, S633, and S686. These sites, particularly within the nuclear localization signal (NLS), control Msn2’s shuttling between cytoplasm and nucleus, impacting its transcriptional activity ([Gallmetzer et al., 2018](https://www.molbiolcell.org/doi/10.1091/mbc.E18-06-0389)).

AlphaFold Model

The structure is an AlphaFold-predicted model, offering a reliable depiction of Msn2’s 704-amino-acid structure. AlphaFold’s deep learning approach predicts the protein’s fold, including the zinc finger domains and regions containing phosphorylation sites, based on the sequence from [UniProt: P33748](https://www.uniprot.org/uniprotkb/P33748/entry).

References

Proteopedia Page Contributors and Editors (what is this?)

Joseph M. Steinberger

Personal tools