1c1z: Difference between revisions
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{{STRUCTURE_1c1z| PDB=1c1z | SCENE= }} | {{STRUCTURE_1c1z| PDB=1c1z | SCENE= }} | ||
===CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)=== | |||
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==About this Structure== | ==About this Structure== | ||
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[[Category: Short consensus repeat]] | [[Category: Short consensus repeat]] | ||
[[Category: Sushi domain]] | [[Category: Sushi domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:05:54 2008'' | |||
Revision as of 17:05, 30 June 2008
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| 1c1z, resolution 2.87Å (default scene) | |||||||||||||
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| Ligands: | BMA, MAN, NDG, NAG | ||||||||||||
| Related: | 1vvc, 1ckl, 1hfh, 1qub | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1C1Z is a Single protein structure of sequence from Homo sapiens. 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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