1n69: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= Prosaposin, PSAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= Prosaposin, PSAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n69 OCA], [http://www.ebi.ac.uk/pdbsum/1n69 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n69 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Prive, G G.]] | [[Category: Prive, G G.]] | ||
[[Category: Whitelegge, J P.]] | [[Category: Whitelegge, J P.]] | ||
[[Category: glycosphingolipid activator protein]] | [[Category: glycosphingolipid activator protein]] | ||
[[Category: lipid binding protein]] | [[Category: lipid binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:25:57 2008'' | ||
