2evq
From Proteopedia
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| - | [[Image:2evq.gif|left|200px]] | + | [[Image:2evq.gif|left|200px]] |
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| - | '''Solution structure of HP7, a 12-residue beta hairpin''' | + | {{Structure |
| + | |PDB= 2evq |SIZE=350|CAPTION= <scene name='initialview01'>2evq</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of HP7, a 12-residue beta hairpin''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2EVQ is a [ | + | 2EVQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVQ OCA]. |
==Reference== | ==Reference== | ||
| - | Minimization and optimization of designed beta-hairpin folds., Andersen NH, Olsen KA, Fesinmeyer RM, Tan X, Hudson FM, Eidenschink LA, Farazi SR, J Am Chem Soc. 2006 May 10;128(18):6101-10. PMID:[http:// | + | Minimization and optimization of designed beta-hairpin folds., Andersen NH, Olsen KA, Fesinmeyer RM, Tan X, Hudson FM, Eidenschink LA, Farazi SR, J Am Chem Soc. 2006 May 10;128(18):6101-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16669679 16669679] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Andersen, N H.]] | [[Category: Andersen, N H.]] | ||
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[[Category: trp/trp packing]] | [[Category: trp/trp packing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:45:07 2008'' |
Revision as of 14:45, 20 March 2008
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Solution structure of HP7, a 12-residue beta hairpin
Overview
Minimized beta hairpins have provided additional data on the geometric preferences of Trp interactions in TW-loop-WT motifs. This motif imparts significant fold stability to peptides as short as 8 residues. High-resolution NMR structures of a 16- (KKWTWNPATGKWTWQE, DeltaG(U)(298) >or= +7 kJ/mol) and 12-residue (KTWNPATGKWTE, DeltaG(U)(298) = +5.05 kJ/mol) hairpin reveal a common turn geometry and edge-to-face (EtF) packing motif and a cation-pi interaction between Lys(1) and the Trp residue nearest the C-terminus. The magnitude of a CD exciton couplet (due to the two Trp residues) and the chemical shifts of a Trp Hepsilon3 site (shifted upfield by 2.4 ppm due to the EtF stacking geometry) provided near-identical measures of folding. CD melts of representative peptides with the -TW-loop-WT- motif provided the thermodynamic parameters for folding, which reflect enthalpically driven folding at laboratory temperatures with a small DeltaC(p) for unfolding (+420 J K(-)(1)/mol). In the case of Asx-Pro-Xaa-Thr-Gly-Xaa loops, mutations established that the two most important residues in this class of direction-reversing loops are Asx and Gly: mutation to alanine is destabilizing by about 6 and 2 kJ/mol, respectively. All indicators of structuring are retained in a minimized 8-residue construct (Ac-WNPATGKW-NH(2)) with the fold stability reduced to DeltaG(U)(278) = -0.7 kJ/mol. NMR and CD comparisons indicate that -TWXNGKWT- (X = S, I) sequences also form the same hairpin-stabilizing W/W interaction.
About this Structure
2EVQ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Minimization and optimization of designed beta-hairpin folds., Andersen NH, Olsen KA, Fesinmeyer RM, Tan X, Hudson FM, Eidenschink LA, Farazi SR, J Am Chem Soc. 2006 May 10;128(18):6101-10. PMID:16669679
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