Nematode Her-1


Nematode Her-1
Caenor_Her-1
PDB 1szh EBI.jpg
crystal structure of c. elegans her-1
Identifiers
Symbol Caenor_Her-1
Pfam PF09232
InterPro IPR015313
SCOP 1szh

In molecular biology the nematode Her-1 protein is a protein which adopts an all-helical structure with two subdomains: amino acids 19-80 comprise a left-handed three-helix bundle with an overhand connection between the second and third helices, whilst amino acids 81-164 comprise a left-handed anti-parallel four-helix bundle in which the first helix consists of four consecutive turns of 3-10-helix. Fourteen cysteines are conserved in all known HER-1 sequences and form seven disulphide bonds. The protein dictates male development in Caenorhabditis elegans, probably by playing a direct role in cell signalling during C. elegans sex determination. It also inhibits the function of tra-2a.[1]

References

This article includes text from the public domain Pfam and InterPro IPR015313


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