Myogenic determination factor 5

In molecular biology, the myogenic determination factor 5 proteins are a family of proteins found in eukaryotes. This family includes the Myf5 protein, which is responsible for directing cells to the skeletal myocyte lineage during development. Myf5 is likely to act in a similar way to the other MRF4 proteins such as MyoD which perform the same function. These are histone acetyltransferases and histone deacetylases which activate and repress genes involved in the myocyte lineage.

Myf5 domain
Identifiers
SymbolMyf5
PfamPF12232
InterProIPR022032
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Basic domain
crystal structure of myod bhlh domain bound to dna: perspectives on dna recognition and implications for transcriptional activation
Identifiers
SymbolBasic
PfamPF01586
InterProIPR002546
PROSITEPDOC00038
SCOP21mdy / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Myogenic determination factor 5 proteins contain three conserved protein domains. A C-terminal Myf5 domain, a central basic helix-loop-helix (bHLH) domain and an N-terminal basic domain. The bHLH region mediates specific DNA binding.[1] With 12 residues of the basic domain involved in DNA binding.[2] The basic domain forms an extended alpha helix in the structure.

References

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  1. ^ Hamamori Y, Wu HY, Sartorelli V, Kedes L (November 1997). "The basic domain of myogenic basic helix-loop-helix (bHLH) proteins is the novel target for direct inhibition by another bHLH protein, Twist". Mol. Cell. Biol. 17 (11): 6563–73. doi:10.1128/mcb.17.11.6563. PMC 232510. PMID 9343420.
  2. ^ Molkentin JD, Olson EN (September 1996). "Combinatorial control of muscle development by basic helix-loop-helix and MADS-box transcription factors". Proc. Natl. Acad. Sci. U.S.A. 93 (18): 9366–73. Bibcode:1996PNAS...93.9366M. doi:10.1073/pnas.93.18.9366. PMC 38433. PMID 8790335.
This article incorporates text from the public domain Pfam and InterPro: IPR022032
This article incorporates text from the public domain Pfam and InterPro: IPR002546