Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Crystal structure of saposin B reveals a dimeric shell for lipid binding.

http://www.ncbi.nlm.nih.gov/pubmed/12518053

Saposin B is a small, nonenzymatic glycosphingolipid activator protein required for the breakdown of cerebroside sulfates (sulfatides) within the lysosome. The protein can extract target lipids from membranes, forming soluble protein-lipid complexes that are recognized by arylsulfatase A. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. Although the secondary structure of saposin B is similar to that of the known monomeric members of the saposin-like superfamily, the helices are repacked into a different tertiary arrangement to form the homodimer. A comparison of the two forms of the saposin B dimer suggests that extraction of target lipids from membranes involves a conformational change that facilitates access to the inner cavity.

Pubmed ID: 12518053 RIS Download

Mesh terms: Amino Acid Sequence | Amino Acid Substitution | Binding Sites | Crystallography, X-Ray | Dimerization | Glycoproteins | Humans | Lipid Metabolism | Models, Molecular | Molecular Sequence Data | Protein Structure, Secondary | Saposins | Sequence Alignment | Sequence Homology, Amino Acid | Sphingolipid Activator Proteins