Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2002-12

AUTHORS

William Mifsud, Alex Bateman

ABSTRACT

BACKGROUND: Membrane-associated progesterone receptors (MAPRs) are thought to mediate a number of rapid cellular effects not involving changes in gene expression. They do not show sequence similarity to any of the classical steroid receptors. We were interested in identifying distant homologs of MAPR better to understand their biological roles. RESULTS: We have identified MAPRs as distant homologs of cytochrome b5. We have also found regions homologous to cytochrome b5 in the mammalian HERC2 ubiquitin transferase proteins and a number of fungal chitin synthases. CONCLUSIONS: In view of these findings, we propose that the heme-binding cytochrome b5 domain served as a template for the evolution of membrane-associated binding pockets for non-heme ligands. More... »

PAGES

research0068.1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/gb-2002-3-12-research0068

DOI

http://dx.doi.org/10.1186/gb-2002-3-12-research0068

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013259310

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12537557


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