%0 Journal Article
%T Crystal structure of the conserved domain of the DC lysosomal associated membrane protein: implications for the lysosomal glycocalyx
%A Sonja Wilke
%A Joern Krausze
%A Konrad Bussow
%J BMC Biology
%D 2012
%I BioMed Central
%R 10.1186/1741-7007-10-62
%X The crystal structure of the conserved domain of human DC-LAMP was solved. It is the first high-resolution structure of a heavily glycosylated lysosomal membrane protein. The structure represents a novel ¦Â-prism fold formed by two ¦Â-sheets bent by ¦Â-bulges and connected by a disulfide bond. Flexible loops and a hydrophobic pocket represent possible sites of molecular interaction. Computational models of the glycosylated luminal regions of LAMP-1 and LAMP-2 indicate that the proteins adopt a compact conformation in close proximity to the lysosomal membrane. The models correspond to the thickness of the lysosomal glycoprotein coat of only 5 to 12 nm, according to electron microscopy.The conserved luminal domain of lysosome-associated membrane proteins forms a previously unknown ¦Â-prism fold. Insights into the structure of the lysosomal glycoprotein coat were obtained by computational models of the LAMP-1 and LAMP-2 luminal regions.
%U http://www.biomedcentral.com/1741-7007/10/62/abstract