Q8N205: Nesprin-4 (SYNE4)

Nesprin-4 (SYNE4) is a 404-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8N205.

Gene
SYNE4
Organism
Homo sapiens
Length
404 residues
Mean pLDDT
57.2
Model
AF-Q8N205-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 57.2 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate14%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution17%
Below 50Very low: often disordered regions54%

What pLDDT means and how to read it

Function

As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Behaves as a kinesin cargo, providing a functional binding site for kinesin-1 at the nuclear envelope. Hence may contribute to the establishment of secretory epithelial morphology by promoting kinesin-dependent apical migration of the centrosome and Golgi apparatus and basal localization of the nucleus (By similarity)

Subunit structure

Core component of LINC complexes which are composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-containing proteins seem to bind each other promiscuously; however, differentially expression of LINC complex constituents can give rise to specific assemblies (By similarity). Probably part of a…

Subcellular location

Nucleus outer membrane

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6WMDX-ray1.5 ÅB=377-404
6R16X-ray2.75 ÅG/H/I/J/K/L=376-404

More AlphaFold highlights

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