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| ==Crystal structure of the anti-HIV b12 scaffold protein== | | ==Crystal structure of the anti-HIV b12 scaffold protein== |
- | <StructureSection load='3rpt' size='340' side='right' caption='[[3rpt]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='3rpt' size='340' side='right'caption='[[3rpt]], [[Resolution|resolution]] 1.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3rpt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RPT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rpt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPT FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.303Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">celB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2021 "Thermonospora fusca" Henssen 1957])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=3rpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rpt OCA], [https://pdbe.org/3rpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rpt RCSB], [https://www.ebi.ac.uk/pdbsum/3rpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rpt 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=3rpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rpt OCA], [http://pdbe.org/3rpt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rpt RCSB], [http://www.ebi.ac.uk/pdbsum/3rpt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rpt ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| ==See Also== | | ==See Also== |
- | *[[Glucanase|Glucanase]] | + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Thermonospora fusca henssen 1957]] | + | [[Category: Large Structures]] |
- | [[Category: Cellulase]] | + | [[Category: Thermobifida fusca]] |
- | [[Category: Chen, L]] | + | [[Category: Chen L]] |
- | [[Category: Kwong, P D]] | + | [[Category: Kwong PD]] |
- | [[Category: Hydrolase]]
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- | [[Category: Scaffold protein anti-hiv]]
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| Structural highlights
Publication Abstract from PubMed
The manipulation of protein backbone structure to control interaction and function is a challenge for protein engineering. We integrated computational design with experimental selection for grafting the backbone and side chains of a two-segment HIV gp120 epitope, targeted by the cross-neutralizing antibody b12, onto an unrelated scaffold protein. The final scaffolds bound b12 with high specificity and with affinity similar to that of gp120, and crystallographic analysis of a scaffold bound to b12 revealed high structural mimicry of the gp120-b12 complex structure. The method can be generalized to design other functional proteins through backbone grafting.
Computation-guided backbone grafting of a discontinuous motif onto a protein scaffold.,Azoitei ML, Correia BE, Ban YE, Carrico C, Kalyuzhniy O, Chen L, Schroeter A, Huang PS, McLellan JS, Kwong PD, Baker D, Strong RK, Schief WR Science. 2011 Oct 21;334(6054):373-6. PMID:22021856[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Azoitei ML, Correia BE, Ban YE, Carrico C, Kalyuzhniy O, Chen L, Schroeter A, Huang PS, McLellan JS, Kwong PD, Baker D, Strong RK, Schief WR. Computation-guided backbone grafting of a discontinuous motif onto a protein scaffold. Science. 2011 Oct 21;334(6054):373-6. PMID:22021856 doi:10.1126/science.1209368
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