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| | ==Nanobody targeting mouse Vsig4 in Spacegroup P3221== | | ==Nanobody targeting mouse Vsig4 in Spacegroup P3221== |
| - | <StructureSection load='5imo' size='340' side='right' caption='[[5imo]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5imo' size='340' side='right'caption='[[5imo]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5imo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelidae Camelidae] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IMO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5imo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelidae Camelidae] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IMO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5imk|5imk]], [[5iml|5iml]], [[5imm|5imm]]</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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vsig4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5imo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5imo OCA], [https://pdbe.org/5imo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5imo RCSB], [https://www.ebi.ac.uk/pdbsum/5imo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5imo ProSAT]</span></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=5imo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5imo OCA], [http://pdbe.org/5imo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5imo RCSB], [http://www.ebi.ac.uk/pdbsum/5imo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5imo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F6TUL9_MOUSE F6TUL9_MOUSE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Camelidae]] | | [[Category: Camelidae]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Wen, Y]] | + | [[Category: Mus musculus]] |
| - | [[Category: Zheng, F]] | + | [[Category: Wen Y]] |
| - | [[Category: Complement receptor]] | + | [[Category: Zheng F]] |
| - | [[Category: Immune system]]
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| - | [[Category: Nanobody]]
| + | |
| - | [[Category: Vsig4 crig]]
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| Structural highlights
Function
F6TUL9_MOUSE
Publication Abstract from PubMed
Vsig4 is a recently identified immune regulatory protein related to the B7 family with dual functionality: a negative regulator of T cell activation and a receptor for the complement components C3b and C3c. Here we present a structural evaluation of a nanobody, Nb119, against the extracellular IgV domain protein of both mouse and human recombinant Vsig4, which have a high degree of sequence identity. Although mouse and human Vsig4 bind to Nb119 with a 250 times difference in dissociation constants, the interaction results in a highly identical assembly with a RMSD of 0.4A. The molecular determinants for Vsig4 recognition and cross reactivity unveiled by the atomic structure of Nb119 in complex with mVsig4 and hVsig4 afford new insights useful for the further optimization of the nanobody for potential use in humans. Additionally, structural analysis of the Vsig4-Nb119 complexes indicates that Nb119 occupies the interface on Vsig4 recognized by the macroglobulin-like domains MG4 and MG5 of C3b. Thus an affinity-improved Nb119 may have the potential to influence the activation of both T cells and complement.
Structural evaluation of a nanobody targeting complement receptor Vsig4 and its cross reactivity.,Wen Y, Ouyang Z, Schoonooghe S, Luo S, De Baetselier P, Lu W, Muyldermans S, Raes G, Zheng F Immunobiology. 2016 Nov 18. pii: S0171-2985(16)30436-3. doi:, 10.1016/j.imbio.2016.11.008. PMID:27889311[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wen Y, Ouyang Z, Schoonooghe S, Luo S, De Baetselier P, Lu W, Muyldermans S, Raes G, Zheng F. Structural evaluation of a nanobody targeting complement receptor Vsig4 and its cross reactivity. Immunobiology. 2016 Nov 18. pii: S0171-2985(16)30436-3. doi:, 10.1016/j.imbio.2016.11.008. PMID:27889311 doi:http://dx.doi.org/10.1016/j.imbio.2016.11.008
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