1c1z

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spinqualitylabelsall models 1c1z, resolution 2.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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 NDG and MAN 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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