5n86
From Proteopedia
(Difference between revisions)
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<StructureSection load='5n86' size='340' side='right' caption='[[5n86]], [[Resolution|resolution]] 1.48Å' scene=''> | <StructureSection load='5n86' size='340' side='right' caption='[[5n86]], [[Resolution|resolution]] 1.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5n86]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N86 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5n86]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N86 FirstGlance]. <br> |
| - | </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=5n86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n86 OCA], [http://pdbe.org/5n86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n86 RCSB], [http://www.ebi.ac.uk/pdbsum/5n86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n86 ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STAB2, FEEL2, FELL, FEX2, HARE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5n86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n86 OCA], [http://pdbe.org/5n86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n86 RCSB], [http://www.ebi.ac.uk/pdbsum/5n86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n86 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/STAB2_HUMAN STAB2_HUMAN]] Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalisation as well as HA and CS.<ref>PMID:12077138</ref> <ref>PMID:12473645</ref> <ref>PMID:15208308</ref> <ref>PMID:15572036</ref> <ref>PMID:17145755</ref> <ref>PMID:17675564</ref> <ref>PMID:17962816</ref> <ref>PMID:18230608</ref> <ref>PMID:18434317</ref> <ref>PMID:18573870</ref> <ref>PMID:19359419</ref> | [[http://www.uniprot.org/uniprot/STAB2_HUMAN STAB2_HUMAN]] Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalisation as well as HA and CS.<ref>PMID:12077138</ref> <ref>PMID:12473645</ref> <ref>PMID:15208308</ref> <ref>PMID:15572036</ref> <ref>PMID:17145755</ref> <ref>PMID:17675564</ref> <ref>PMID:17962816</ref> <ref>PMID:18230608</ref> <ref>PMID:18434317</ref> <ref>PMID:18573870</ref> <ref>PMID:19359419</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Recent research has identified a potential role of the hyaluronic acid receptor stabilin-2 (Stab2) in cancer metastasis. Stab2 belongs to a group of scavenger receptors and is responsible for the clearance of more than ten ligands, including hyaluronic acid (HA). In vivo experiments on mice have shown that the absence of Stab2, or its blocking by an antibody, effectively opposes cancer metastasis, which is accompanied by an increase in the level of circulating HA. Knowledge of ligand recognition and signal transduction by Stab2 is limited and no three-dimensional structures of any protein fragments of this receptor have been solved to date. Here, a high-resolution X-ray structure of the seventh FAS1 domain of Stab2 is reported. This structure provides the first insight into the Stab2 structure. | ||
| + | |||
| + | Crystal structure of the FAS1 domain of the hyaluronic acid receptor stabilin-2.,Twarda-Clapa A, Labuzek B, Krzemien D, Musielak B, Grudnik P, Dubin G, Holak TA Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):695-701. doi:, 10.1107/S2059798318007271. Epub 2018 Jun 27. PMID:29968679<ref>PMID:29968679</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5n86" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Dubin, G]] | [[Category: Dubin, G]] | ||
[[Category: Grudnik, P]] | [[Category: Grudnik, P]] | ||
Revision as of 06:04, 11 July 2018
Crystal structure of FAS1 domain of hyaluronic acid receptor stabilin-2
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