4ccv
Crystal structure of histidine-rich glycoprotein N2 domain reveals redox activity at an interdomain disulfide bridge: Implications for the regulation of angiogenesisCrystal structure of histidine-rich glycoprotein N2 domain reveals redox activity at an interdomain disulfide bridge: Implications for the regulation of angiogenesis
Template:ABSTRACT PUBMED 24501222
FunctionFunction
[HRG_RABIT] Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Inhibits rosette formation. Acts as an adapter protein and implicated in regulating many processes such as immune complex and pathogen clearance, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Binds T-cells and alters the cell morphology Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2 (By similarity). Tethers plasminogen to the cell surface.[1]
About this StructureAbout this Structure
4ccv is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Kassaar O, McMahon SA, Thompson R, Botting CH, Naismith JH, Stewart AJ. Crystal structure of histidine-rich glycoprotein N2 domain reveals redox activity at an interdomain disulfide bridge: implications for angiogenic regulation. Blood. 2014 Feb 5. PMID:24501222 doi:http://dx.doi.org/10.1182/blood-2013-11-535963
- ↑ Juarez JC, Guan X, Shipulina NV, Plunkett ML, Parry GC, Shaw DE, Zhang JC, Rabbani SA, McCrae KR, Mazar AP, Morgan WT, Donate F. Histidine-proline-rich glycoprotein has potent antiangiogenic activity mediated through the histidine-proline-rich domain. Cancer Res. 2002 Sep 15;62(18):5344-50. PMID:12235005