1c1z: Difference between revisions
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[[Image:1c1z.png|left|200px]] | [[Image:1c1z.png|left|200px]] | ||
{{STRUCTURE_1c1z| PDB=1c1z | SCENE= }} | {{STRUCTURE_1c1z| PDB=1c1z | SCENE= }} | ||
===CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)=== | ===CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)=== | ||
{{ABSTRACT_PUBMED_10562535}} | {{ABSTRACT_PUBMED_10562535}} | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:010562535</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Diederichs, K.]] | [[Category: Diederichs, K.]] | ||
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[[Category: Schwarzenbacher, R.]] | [[Category: Schwarzenbacher, R.]] | ||
[[Category: Zeth, K.]] | [[Category: Zeth, K.]] | ||
[[Category: Ccp]] | |||
[[Category: Complement control protein module]] | |||
[[Category: Glycoprotein]] | |||
[[Category: Scr]] | |||
[[Category: Short consensus repeat]] | |||
[[Category: Signaling protein]] | |||
[[Category: Sushi domain]] | |||
Revision as of 23:54, 21 October 2012
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| 1c1z, resolution 2.87Å () | |||||||||
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| Ligands: | , , , | ||||||||
| 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)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 StructureAbout this Structure
1c1z is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Schwarzenbacher R, Zeth K, Diederichs K, Gries A, Kostner GM, Laggner P, Prassl R. Crystal structure of human beta2-glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome. EMBO J. 1999 Nov 15;18(22):6228-39. PMID:10562535 doi:10.1093/emboj/18.22.6228