1n69
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(New page: 200px<br /> <applet load="1n69" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n69, resolution 2.20Å" /> '''Crystal structure o...)
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Revision as of 16:11, 12 November 2007
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Crystal structure of human saposin B
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Combined SAP deficiency OMIM:[176801], Gaucher disease, atypical OMIM:[176801], Metachromatic leukodystrophy due to deficiency of SAP-1 OMIM:[176801]
About this Structure
1N69 is a Single protein structure of sequence from Homo sapiens with PEH as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of saposin B reveals a dimeric shell for lipid binding., Ahn VE, Faull KF, Whitelegge JP, Fluharty AL, Prive GG, Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):38-43. Epub 2002 Dec 23. PMID:12518053
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