Nematode Her-1

Available protein structures:
PDB	IPR015313 PF09232 (ECOD; PDBsum)
AlphaFold	IPR015313; PF09232;

Caenor_Her-1
Caenor_Her-1
	crystal structure of c. elegans her-1
Identifiers
Symbol	Caenor_Her-1
Pfam	PF09232
InterPro	IPR015313
SCOP2	1szh / SCOPe / SUPFAM
PDB
Available protein structures:
PDB	IPR015313 PF09232 (ECOD; PDBsum)
AlphaFold	IPR015313; PF09232;

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

^ Hamaoka BY, Dann CE, Geisbrecht BV, Leahy DJ (August 2004). "Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A". Proc. Natl. Acad. Sci. U.S.A. 101 (32): 11673–8. doi:10.1073/pnas.0402559101. PMC 511037. PMID 15289613.

This article incorporates text from the public domain Pfam and InterPro: IPR015313

[pmid15289613-1] Hamaoka BY, Dann CE, Geisbrecht BV, Leahy DJ (August 2004). "Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A". Proc. Natl. Acad. Sci. U.S.A. 101 (32): 11673–8. doi:10.1073/pnas.0402559101. PMC 511037. PMID 15289613.

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