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2xee

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Revision as of 10:51, 13 April 2022

Structural Determinants for Improved Thermal Stability of Designed Ankyrin Repeat Proteins With a Redesigned C-capping Module.

Structural highlights

2xee is a 4 chain structure with sequence from Synthetic construct sequences. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Designed ankyrin-repeat proteins (DARPins) that specifically bind to almost any target can be obtained by ribosome display or phage display from combinatorial libraries. Although DARPins are already very stable molecules, molecular dynamics simulations, equilibrium denaturation experiments, structural studies, and recent NMR experiments suggested that the unfolding of the original C-terminal capping repeat (C-cap), taken from a natural ankyrin repeat protein, limits the stability of the initial DARPin design. Several point mutations had been introduced to optimize the C-cap and were shown to indeed further increase the stability of DARPins. We now determined crystal structures of DARPins with one or three full-consensus internal repeats (NI(1)C or NI(3)C) between an N-cap and mutants of the C-cap. An NI(1)C mutant, in which the C-cap was only extended by three additional helix-forming residues, showed no structural change, but reduced B-factors in the C-cap. An NI(3)C C-cap mutant carrying five additional mutations in the interface to the preceding repeat, previously designed by using the consensus sequence as a guide, showed a rigid body movement of the C-cap towards the internal repeat. This movement results in an increased buried surface area, a superior surface complementarity and explains the improved stability in equilibrium unfolding, compared to the original C-cap. A C-cap mutant with three additional mutations introducing suitably spaced charged residues did not show formation of salt bridges, explaining why its stability was not increased further. These structural studies underline the importance of repeat coupling for stability and help in the further design of this protein family.

Structural Determinants for Improved Stability of Designed Ankyrin Repeat Proteins With a Redesigned C-capping Module.,Kramer MA, Wetzel SK, Pluckthun A, Mittl PR, Grutter MG J Mol Biol. 2010 Sep 16. PMID:20851127^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kramer MA, Wetzel SK, Pluckthun A, Mittl PR, Grutter MG. Structural Determinants for Improved Stability of Designed Ankyrin Repeat Proteins With a Redesigned C-capping Module. J Mol Biol. 2010 Sep 16. PMID:20851127 doi:10.1016/j.jmb.2010.09.023

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xee"

@@ Line 3: / Line 3: @@
 <StructureSection load='2xee' size='340' side='right'caption='[[2xee]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xee]] is a 4 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=2XEE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XEE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xee]] is a 4 chain structure with sequence from [https://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=2XEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XEE FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xee OCA], [http://pdbe.org/2xee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xee RCSB], [http://www.ebi.ac.uk/pdbsum/2xee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xee ProSAT]</span></td></tr>
+</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=2xee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xee OCA], [https://pdbe.org/2xee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xee RCSB], [https://www.ebi.ac.uk/pdbsum/2xee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xee ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

2xee

From Proteopedia

Revision as of 10:51, 13 April 2022

Structural Determinants for Improved Thermal Stability of Designed Ankyrin Repeat Proteins With a Redesigned C-capping Module.

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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