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2M9J

NMR solution structure of Pin1 WW domain mutant 6-1g

Summary for 2M9J
Entry DOI10.2210/pdb2m9j/pdb
Related2M9E 2M9F 2M9I
NMR InformationBMRB: 19296
DescriptorPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
Functional Keywordsn-glycosylation, enhanced aromatic sequon, ww domain, ch-pi interaction, isomerase
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight4243.72
Authors
Enck, S.,Chen, W.,Price, J.L.,Powers, E.T.,Wong, C.,Dyson, H.J.,Kelly, J.W. (deposition date: 2013-06-10, release date: 2013-06-26, Last modification date: 2020-07-29)
Primary citationChen, W.,Enck, S.,Price, J.L.,Powers, D.L.,Powers, E.T.,Wong, C.H.,Dyson, H.J.,Kelly, J.W.
Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins.
J.Am.Chem.Soc., 135:9877-9884, 2013
Cited by
PubMed Abstract: Carbohydrate-aromatic interactions mediate many biological processes. However, the structure-energy relationships underpinning direct carbohydrate-aromatic packing interactions in aqueous solution have been difficult to assess experimentally and remain elusive. Here, we determine the structures and folding energetics of chemically synthesized glycoproteins to quantify the contributions of the hydrophobic effect and CH-π interactions to carbohydrate-aromatic packing interactions in proteins. We find that the hydrophobic effect contributes significantly to protein-carbohydrate interactions. Interactions between carbohydrates and aromatic amino acid side chains, however, are supplemented by CH-π interactions. The strengths of experimentally determined carbohydrate CH-π interactions do not correlate with the electrostatic properties of the involved aromatic residues, suggesting that the electrostatic component of CH-π interactions in aqueous solution is small. Thus, tight binding of carbohydrates and aromatic residues is driven by the hydrophobic effect and CH-π interactions featuring a dominating dispersive component.
PubMed: 23742246
DOI: 10.1021/ja4040472
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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