5mfc: Difference between revisions
New page: '''Unreleased structure''' The entry 5mfc is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==Designed armadillo repeat protein YIIIM5AII in complex with (KR)4-GFP== | |||
<StructureSection load='5mfc' size='340' side='right'caption='[[5mfc]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5mfc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MFC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></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=5mfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mfc OCA], [https://pdbe.org/5mfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mfc RCSB], [https://www.ebi.ac.uk/pdbsum/5mfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mfc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A059PIQ0_AEQVI A0A059PIQ0_AEQVI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Designed armadillo repeat proteins (dArmRP) are alpha-helical solenoid repeat proteins with an extended peptide binding groove that were engineered to develop a generic modular technology for peptide recognition. In this context, the term "peptide" not only denotes a short unstructured chain of amino acids, but also an unstructured region of a protein, as they occur in termini, loops, or linkers between folded domains. Here we report two crystal structures of dArmRPs, in complex with peptides fused either to the N-terminus of Green Fluorescent Protein or to the C-terminus of a phage lambda protein D. These structures demonstrate that dArmRPs bind unfolded peptides in the intended conformation also when they constitute unstructured parts of folded proteins, which greatly expands possible applications of the dArmRP technology. Nonetheless, the structures do not fully reflect the binding behavior in solution, that is, some binding sites remain unoccupied in the crystal and even unexpected peptide residues appear to be bound. We show how these differences can be explained by restrictions of the crystal lattice or the composition of the crystallization solution. This illustrates that crystal structures have to be interpreted with caution when protein-peptide interactions are characterized, and should always be correlated with measurements in solution. | |||
Structures of designed armadillo repeat proteins binding to peptides fused to globular domains.,Hansen S, Kiefer JD, Madhurantakam C, Mittl PRE, Pluckthun A Protein Sci. 2017 Oct;26(10):1942-1952. doi: 10.1002/pro.3229. Epub 2017 Jul 25. PMID:28691351<ref>PMID:28691351</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5mfc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aequorea victoria]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Hansen S]] | |||
[[Category: Kiefer J]] | |||
[[Category: Madhurantakam C]] | |||
[[Category: Mittl P]] | |||
[[Category: Plueckthun A]] | |||
Latest revision as of 21:41, 1 November 2023
Designed armadillo repeat protein YIIIM5AII in complex with (KR)4-GFPDesigned armadillo repeat protein YIIIM5AII in complex with (KR)4-GFP
Structural highlights
FunctionPublication Abstract from PubMedDesigned armadillo repeat proteins (dArmRP) are alpha-helical solenoid repeat proteins with an extended peptide binding groove that were engineered to develop a generic modular technology for peptide recognition. In this context, the term "peptide" not only denotes a short unstructured chain of amino acids, but also an unstructured region of a protein, as they occur in termini, loops, or linkers between folded domains. Here we report two crystal structures of dArmRPs, in complex with peptides fused either to the N-terminus of Green Fluorescent Protein or to the C-terminus of a phage lambda protein D. These structures demonstrate that dArmRPs bind unfolded peptides in the intended conformation also when they constitute unstructured parts of folded proteins, which greatly expands possible applications of the dArmRP technology. Nonetheless, the structures do not fully reflect the binding behavior in solution, that is, some binding sites remain unoccupied in the crystal and even unexpected peptide residues appear to be bound. We show how these differences can be explained by restrictions of the crystal lattice or the composition of the crystallization solution. This illustrates that crystal structures have to be interpreted with caution when protein-peptide interactions are characterized, and should always be correlated with measurements in solution. Structures of designed armadillo repeat proteins binding to peptides fused to globular domains.,Hansen S, Kiefer JD, Madhurantakam C, Mittl PRE, Pluckthun A Protein Sci. 2017 Oct;26(10):1942-1952. doi: 10.1002/pro.3229. Epub 2017 Jul 25. PMID:28691351[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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