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| | <StructureSection load='4v3r' size='340' side='right'caption='[[4v3r]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='4v3r' size='340' side='right'caption='[[4v3r]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v3r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V3R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v3r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V3R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v3o|4v3o]], [[4v3q|4v3q]]</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=4v3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3r OCA], [https://pdbe.org/4v3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v3r RCSB], [https://www.ebi.ac.uk/pdbsum/4v3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v3r 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=4v3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v3r OCA], [http://pdbe.org/4v3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v3r RCSB], [http://www.ebi.ac.uk/pdbsum/4v3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v3r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Synthetic construct sequences]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Madhurantakam, C]] | + | [[Category: Madhurantakam C]] |
| - | [[Category: Mittl, P]] | + | [[Category: Mittl P]] |
| - | [[Category: Pluckthun, A]] | + | [[Category: Pluckthun A]] |
| - | [[Category: Reichen, C]] | + | [[Category: Reichen C]] |
| - | [[Category: De novo protein]]
| + | |
| - | [[Category: Protein engineering]]
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| - | [[Category: Repeat protein]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The armadillo repeat serves as a scaffold for the development of modular peptide-recognition modules. In order to develop such a system, three crystal structures of designed armadillo-repeat proteins with third-generation N-caps (YIII-type), four or five internal repeats (M-type) and second-generation C-caps (AII-type) were determined at 1.8 A (His-YIIIM4AII), 2.0 A (His-YIIIM5AII) and 1.95 A (YIIIM5AII) resolution and compared with those of variants with third-generation C-caps. All constructs are full consensus designs in which the internal repeats have exactly the same sequence, and hence identical conformations of the internal repeats are expected. The N-cap and internal repeats M1 to M3 are indeed extremely similar, but the comparison reveals structural differences in internal repeats M4 and M5 and the C-cap. These differences are caused by long-range effects of the C-cap, contacting molecules in the crystal, and the intrinsic design of the repeat. Unfortunately, the rigid-body movement of the C-terminal part impairs the regular arrangement of internal repeats that forms the putative peptide-binding site. The second-generation C-cap improves the packing of buried residues and thereby the stability of the protein. These considerations are useful for future improvements of an armadillo-repeat-based peptide-recognition system.
Structures of designed armadillo-repeat proteins show propagation of inter-repeat interface effects.,Reichen C, Madhurantakam C, Hansen S, Grutter MG, Pluckthun A, Mittl PR Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):168-75. doi:, 10.1107/S2059798315023116. Epub 2016 Jan 1. PMID:26894544[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Reichen C, Madhurantakam C, Hansen S, Grutter MG, Pluckthun A, Mittl PR. Structures of designed armadillo-repeat proteins show propagation of inter-repeat interface effects. Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):168-75. doi:, 10.1107/S2059798315023116. Epub 2016 Jan 1. PMID:26894544 doi:http://dx.doi.org/10.1107/S2059798315023116
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