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| | <StructureSection load='6o5e' size='340' side='right'caption='[[6o5e]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='6o5e' size='340' side='right'caption='[[6o5e]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o5e]] 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=6O5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O5E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o5e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O5E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VTN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6o5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o5e OCA], [http://pdbe.org/6o5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o5e RCSB], [http://www.ebi.ac.uk/pdbsum/6o5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o5e ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6o5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o5e OCA], [https://pdbe.org/6o5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o5e RCSB], [https://www.ebi.ac.uk/pdbsum/6o5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o5e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VTNC_HUMAN VTNC_HUMAN]] Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity. | + | [https://www.uniprot.org/uniprot/VTNC_HUMAN VTNC_HUMAN] Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lechtenberg, B C]] | + | [[Category: Lechtenberg BC]] |
| - | [[Category: Marassi, F M]] | + | [[Category: Marassi FM]] |
| - | [[Category: Shin, K]] | + | [[Category: Shin K]] |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Hemopexin-like domain]]
| + | |
| - | [[Category: Integrin ligand]]
| + | |
| - | [[Category: Serum protein]]
| + | |
| Structural highlights
6o5e is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.9Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
VTNC_HUMAN Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.
Publication Abstract from PubMed
Vitronectin (Vn) is a major component of blood that controls many processes central to human biology. It is a drug target and a key factor in cell and tissue engineering applications, but despite long-standing efforts, little is known about the molecular basis for its functions. Here, we define the domain organization of Vn, report the crystal structure of its carboxyl-terminal domain, and show that it harbors the binding site for the Yersinia pestis outer membrane protein Ail, which recruits Vn to the bacterial cell surface to evade human host defenses. Vn forms a single four-bladed beta/alpha-propeller that serves as a hub for multiple functions. The structure explains key features of native Vn and provides a blueprint for understanding and targeting this essential human protein.
Structure of human Vitronectin C-terminal domain and interaction with Yersinia pestis outer membrane protein Ail.,Shin K, Lechtenberg BC, Fujimoto LM, Yao Y, Bartra SS, Plano GV, Marassi FM Sci Adv. 2019 Sep 11;5(9):eaax5068. doi: 10.1126/sciadv.aax5068. eCollection 2019, Sep. PMID:31535027[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shin K, Lechtenberg BC, Fujimoto LM, Yao Y, Bartra SS, Plano GV, Marassi FM. Structure of human Vitronectin C-terminal domain and interaction with Yersinia pestis outer membrane protein Ail. Sci Adv. 2019 Sep 11;5(9):eaax5068. doi: 10.1126/sciadv.aax5068. eCollection 2019, Sep. PMID:31535027 doi:http://dx.doi.org/10.1126/sciadv.aax5068
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