1c1z
From Proteopedia
(New page: 200px<br /> <applet load="1c1z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c1z, resolution 2.87Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1c1z.gif|left|200px]]<br /> | + | [[Image:1c1z.gif|left|200px]]<br /><applet load="1c1z" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1c1z" size=" | + | |
caption="1c1z, resolution 2.87Å" /> | caption="1c1z, resolution 2.87Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The high affinity of human plasma beta2-glycoprotein I (beta(2)GPI), also | + | The high affinity of human plasma beta2-glycoprotein I (beta(2)GPI), also known as apolipoprotein-H (ApoH), for negatively charged phospholipids determines its implication in a variety of physiological pathways, including blood coagulation and the immune response. beta(2)GPI is considered to be a cofactor for the binding of serum autoantibodies from antiphospholipid syndrome (APS) and correlated with thrombosis, lupus erythematosus and recurrent fetal loss. We solved the beta(2)GPI structure from a crystal form with 84% solvent and present a model containing all 326 amino acid residues and four glycans. The structure reveals four complement control protein modules and a distinctly folding fifth C-terminal domain arranged like beads on a string to form an elongated J-shaped molecule. Domain V folds into a central beta-spiral of four antiparallel beta-sheets with two small helices and an extended C-terminal loop region. It carries a distinct positive charge and the sequence motif CKNKEKKC close to the hydrophobic loop composed of residues LAFW (313-316), resulting in an excellent counterpart for interactions with negatively charged amphiphilic substances. The beta(2)GPI structure reveals potential autoantibody-binding sites and supports mutagenesis studies where Trp316 and CKNKEKKC have been found to be essential for the phospholipid-binding capacity of beta(2)GPI. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C1Z 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 NDG and MAN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1C1Z 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=NDG:'>NDG</scene> and <scene name='pdbligand=MAN:'>MAN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Diederichs, K.]] | [[Category: Diederichs, K.]] | ||
[[Category: Gries, A.]] | [[Category: Gries, A.]] | ||
| - | [[Category: Kostner, G | + | [[Category: Kostner, G M.]] |
[[Category: Laggner, P.]] | [[Category: Laggner, P.]] | ||
[[Category: Prassl, R.]] | [[Category: Prassl, R.]] | ||
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[[Category: sushi domain]] | [[Category: sushi domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:39 2008'' |
Revision as of 10:01, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)
Contents |
Overview
The high affinity of human plasma beta2-glycoprotein I (beta(2)GPI), also known as apolipoprotein-H (ApoH), for negatively charged phospholipids determines its implication in a variety of physiological pathways, including blood coagulation and the immune response. beta(2)GPI is considered to be a cofactor for the binding of serum autoantibodies from antiphospholipid syndrome (APS) and correlated with thrombosis, lupus erythematosus and recurrent fetal loss. We solved the beta(2)GPI structure from a crystal form with 84% solvent and present a model containing all 326 amino acid residues and four glycans. The structure reveals four complement control protein modules and a distinctly folding fifth C-terminal domain arranged like beads on a string to form an elongated J-shaped molecule. Domain V folds into a central beta-spiral of four antiparallel beta-sheets with two small helices and an extended C-terminal loop region. It carries a distinct positive charge and the sequence motif CKNKEKKC close to the hydrophobic loop composed of residues LAFW (313-316), resulting in an excellent counterpart for interactions with negatively charged amphiphilic substances. The beta(2)GPI structure reveals potential autoantibody-binding sites and supports mutagenesis studies where Trp316 and CKNKEKKC have been found to be essential for the phospholipid-binding capacity of beta(2)GPI.
Disease
Known disease associated with this structure: Apolipoprotein H deficiency OMIM:[138700]
About this Structure
1C1Z is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of human beta2-glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome., Schwarzenbacher R, Zeth K, Diederichs K, Gries A, Kostner GM, Laggner P, Prassl R, EMBO J. 1999 Nov 15;18(22):6228-39. PMID:10562535
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