Structural commonalities among integral membrane enzymes

Academic Article

• Overview
• Research
• Identity
• Additional Document Info
• View All

Overview

authors

• Bracey, M. H.
• Cravatt, Benjamin
• Stevens, Raymond

publication date

• June 2004

journal

• FEBS Letters  Journal

abstract

• The X-ray crystal structures of five distinct enzymes (prostaglandin H(2) synthase, squalene cyclase, fatty acid amide hydrolase, microsomal cytochrome P450, and estrone sulfatase) challenge contemporary descriptions of integral membrane proteins. This structurally divergent group represents an important component of the integral membrane proteome that lies at the bilayer's aqueous interface. We summarize here what is collectively understood about the membrane insertion of these proteins, what roles they may play in lipid biology, and their relationship to soluble structural homologs.

subject areas

• Animals
• Crystallography, X-Ray
• Enzymes
• Humans
• Membrane Proteins
• Models, Molecular
• Protein Conformation

Research

keywords

• membrane proteins
• protein structure

Identity

International Standard Serial Number (ISSN)

• 0014-5793

Digital Object Identifier (DOI)

• 10.1016/j.febslet.2004.04.084

PubMed ID

• 15178315

Additional Document Info

start page

• 159

end page

• 165

volume

• 567

issue

• 2-3