2dob
From Proteopedia
(New page: 200px<br /> <applet load="2dob" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dob, resolution 2.00Å" /> '''Crystal Structure o...) |
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| - | [[Image:2dob.gif|left|200px]]<br /> | + | [[Image:2dob.gif|left|200px]]<br /><applet load="2dob" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2dob" size=" | + | |
caption="2dob, resolution 2.00Å" /> | caption="2dob, resolution 2.00Å" /> | ||
'''Crystal Structure of Human Saposin A'''<br /> | '''Crystal Structure of Human Saposin A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Saposins A and C are sphingolipid activator proteins required for the | + | Saposins A and C are sphingolipid activator proteins required for the lysosomal breakdown of galactosylceramide and glucosylceramide, respectively. The saposins interact with lipids, leading to an enhanced accessibility of the lipid headgroups to their cognate hydrolases. We have determined the crystal structures of human saposins A and C to 2.0 Angstroms and 2.4 Angstroms, respectively, and both reveal the compact, monomeric saposin fold. We confirmed that these two proteins were monomeric in solution at pH 7.0 by analytical centrifugation. However, at pH 4.8, in the presence of the detergent C(8)E(5), saposin A assembled into dimers, while saposin C formed trimers. Saposin B was dimeric under all conditions tested. The self-association of the saposins is likely to be relevant to how these small proteins interact with lipids, membranes, and hydrolase enzymes. |
==Disease== | ==Disease== | ||
| - | Known diseases associated with this structure: Combined SAP deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176801 176801]], Gaucher disease, atypical OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176801 176801]], Metachromatic leukodystrophy due to | + | Known diseases associated with this structure: Combined SAP deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176801 176801]], Gaucher disease, atypical OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176801 176801]], Krabbe disease, atypical OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176801 176801]], Metachromatic leukodystrophy due to SAP-b deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176801 176801]] |
==About this Structure== | ==About this Structure== | ||
| - | 2DOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2DOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DOB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ahn, V | + | [[Category: Ahn, V E.]] |
| - | [[Category: Prive, G | + | [[Category: Prive, G G.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: lipid-binding protein]] | [[Category: lipid-binding protein]] | ||
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[[Category: sphingolipid activator protein]] | [[Category: sphingolipid activator protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:00:56 2008'' |
Revision as of 15:00, 21 February 2008
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Crystal Structure of Human Saposin A
Contents |
Overview
Saposins A and C are sphingolipid activator proteins required for the lysosomal breakdown of galactosylceramide and glucosylceramide, respectively. The saposins interact with lipids, leading to an enhanced accessibility of the lipid headgroups to their cognate hydrolases. We have determined the crystal structures of human saposins A and C to 2.0 Angstroms and 2.4 Angstroms, respectively, and both reveal the compact, monomeric saposin fold. We confirmed that these two proteins were monomeric in solution at pH 7.0 by analytical centrifugation. However, at pH 4.8, in the presence of the detergent C(8)E(5), saposin A assembled into dimers, while saposin C formed trimers. Saposin B was dimeric under all conditions tested. The self-association of the saposins is likely to be relevant to how these small proteins interact with lipids, membranes, and hydrolase enzymes.
Disease
Known diseases associated with this structure: Combined SAP deficiency OMIM:[176801], Gaucher disease, atypical OMIM:[176801], Krabbe disease, atypical OMIM:[176801], Metachromatic leukodystrophy due to SAP-b deficiency OMIM:[176801]
About this Structure
2DOB is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of saposins A and C., Ahn VE, Leyko P, Alattia JR, Chen L, Prive GG, Protein Sci. 2006 Aug;15(8):1849-57. Epub 2006 Jul 5. PMID:16823039
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