4ccv

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m (Protected "4ccv" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4ccv| PDB=4ccv | SCENE= }}
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===Crystal structure of histidine-rich glycoprotein N2 domain reveals redox activity at an interdomain disulfide bridge: Implications for the regulation of angiogenesis===
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{{ABSTRACT_PUBMED_24501222}}
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The entry 4ccv is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/HRG_RABIT 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.<ref>PMID:12235005</ref>
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Authors: McMahon, S.A., Kassaar, O., Stewart, A.J., Naismith, J.H.
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==About this Structure==
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[[4ccv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCV OCA].
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Description: Crystal structure of histidine-rich glycoprotein N2 domain reveals redox activity at an interdomain disulfide bridge: Implications for the regulation of angiogenesis
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==Reference==
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<ref group="xtra">PMID:024501222</ref><references group="xtra"/><references/>
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[[Category: Oryctolagus cuniculus]]
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[[Category: Kassaar, O.]]
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[[Category: McMahon, S A.]]
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[[Category: Naismith, J H.]]
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[[Category: Stewart, A J.]]
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[[Category: Blood clotting]]
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[[Category: Coagulation]]
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[[Category: Cystatin]]
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[[Category: S-glutathionylation]]

Revision as of 17:32, 19 February 2014

Template:STRUCTURE 4ccv

Contents

Crystal 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

Function

[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 Structure

4ccv is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

  • 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
  1. ↑ 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

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OCA

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