Sandbox109
This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!
J Polak, 3/3/09:
Those of you who took Chem 391A last semester will recognize this protein from the presentation of research proposal. Those of you who aren't lame-faces, that is.
This green link shows the alpha helices of this protein as green ribbons. For useful contrast, everything else is shown as wireframe in whatever lame default colors they were in.
This green link shows a hydrophobic loop which plays a key role in the protein's phospolipid binding capabilities.
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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 | ||||||||
Text Stolen From Auto-Seeded PageText Stolen From Auto-Seeded Page
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 of sequence from Homo sapiens. Full crystallographic information is available from OCA.
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