Determination of the Border between the Transmembrane and Cytoplasmic Domains of Human Integrin Subunits

Annika Armulik; IngMarie Nilsson; Gunnar von Heijne; Staffan Johansson

doi:10.1074/jbc.274.52.37030

Abstract

In this study we have determined the position of the C-terminal end of the transmembrane domains of human integrin subunits (alpha2, alpha5, beta1, beta2) in microsomal membranes using the glycosylation mapping technique. In contrast to the common view, the transmembrane helices were found to extend roughly to Phe(1129) in alpha2, to Phe(1026) in alpha5, to Ile(757) in beta1, and to His(728) in beta2. The alpha-carbon of the conserved lysine present near the C-terminal end of the transmembrane helix (Lys(1125) in alpha2, Lys(1022) in alpha5, Lys(752) in beta1, and Lys(724) in beta2) is buried in the plasma membrane, and the charged amino group most likely reaches into the polar head-group region of the lipid bilayer. A possible role for the conserved lysine in integrin function is discussed.

Keywords

Transmembrane proteinTransmembrane domainChemistryLipid bilayerMembraneIntegrinLysineCrystallographyAmino acidStereochemistryBiochemistryCell

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Publication Info

Year: 1999
Type: article
Volume: 274
Issue: 52
Pages: 37030-37034
Citations: 84
Access: Closed

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APA Style

                            
                                
                                    Annika Armulik, 
                                
                                    IngMarie Nilsson, 
                                
                                    Gunnar von Heijne
                                
                                et al.
                            
                            (1999). 
                            Determination of the Border between the Transmembrane and Cytoplasmic Domains of Human Integrin Subunits. 
                            Journal of Biological Chemistry
                            , 274
                            (52)
                            , 37030-37034.
                            https://doi.org/10.1074/jbc.274.52.37030
                        

Identifiers

DOI: 10.1074/jbc.274.52.37030