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4ccv
From Proteopedia
(Difference between revisions)
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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== | |
| - | + | <StructureSection load='4ccv' size='340' side='right' caption='[[4ccv]], [[Resolution|resolution]] 1.93Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ccv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ccv RCSB], [http://www.ebi.ac.uk/pdbsum/4ccv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Histidine-rich glycoprotein (HRG) is a plasma protein consisting of six distinct functional domains and is an important regulator of key cardiovascular processes, including angiogenesis and coagulation. The protein is composed of two N-terminal domains (N1 and N2), two proline-rich regions (PRR1 and PRR2) which flank a histidine-rich region (HRR), and a C-terminal domain. To date structural information of HRG has largely come from sequence analysis and spectroscopic studies. It is thought that an HRG fragment containing the HRR, released via plasmin-mediated cleavage, acts as a negative regulator of angiogenesis in vivo. However, its release also requires cleavage of a disulphide bond suggesting that its activity is mediated by a redox process. Here, we present a 1.93 A resolution crystal structure of the N2 domain of serum-purified rabbit HRG. The structure confirms that the N2 domain, which along with the N1 domain forms an important molecular interaction site on HRG, possesses a cystatin-like fold composed of a five-stranded anti-parallel beta-sheet wrapped around a five-turn alpha-helix. A native N-linked glycosylation site was identified at Asn184. Moreover, the structure reveals the presence of an S-glutathionyl adduct at Cys185, which has implications for the redox-mediated release of the anti-angiogenic cleavage product from HRG. | ||
| - | + | Crystal structure of histidine-rich glycoprotein N2 domain reveals redox activity at an interdomain disulfide bridge: implications for angiogenic regulation.,Kassaar O, McMahon SA, Thompson R, Botting CH, Naismith JH, Stewart AJ Blood. 2014 Feb 5. PMID:24501222<ref>PMID:24501222</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | [[Category: Kassaar, O | + | [[Category: Kassaar, O]] |
| - | [[Category: McMahon, S A | + | [[Category: McMahon, S A]] |
| - | [[Category: Naismith, J H | + | [[Category: Naismith, J H]] |
| - | [[Category: Stewart, A J | + | [[Category: Stewart, A J]] |
[[Category: Blood clotting]] | [[Category: Blood clotting]] | ||
[[Category: Coagulation]] | [[Category: Coagulation]] | ||
[[Category: Cystatin]] | [[Category: Cystatin]] | ||
[[Category: S-glutathionylation]] | [[Category: S-glutathionylation]] | ||
Revision as of 18:54, 21 December 2014
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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