ArticleActa crystallographica. Section D, Biological crystallography2013
Evidence for small-molecule-mediated loop stabilization in the structure of the isolated Pin1 WW domain.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- Identification of novel functional mini-receptors by combinatorial screening of split-WW domains.Chemical science · 2022Article
- Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.Chembiochem : a European journal of chemical biology · 2018Article
- The Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.Journal of the American Chemical Society · 2016Article
- Evidence for phenylalanine zipper-mediated dimerization in the X-ray crystal structure of a magainin 2 analogue.Journal of the American Chemical Society · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The human Pin1 WW domain is a small autonomously folding protein that has been useful as a model system for biophysical studies of β-sheet folding. This domain has resisted previous attempts at crystallization for X-ray diffraction studies, perhaps because of intrinsic conformational flexibility that interferes with the formation of a crystal lattice. Here, the crystal structure of the human Pin1 WW domain has been obtained via racemic crystallization in the presence of small-molecule additives. Both enantiomers of a 36-residue variant of the Pin1 WW domain were synthesized chemically, and the L- and D-polypeptides were combined to afford diffracting crystals. The structural data revealed packing interactions of small carboxylic acids, either achiral citrate or a D,L mixture of malic acid, with a mobile loop region of the WW-domain fold. These interactions with solution additives may explain our success in crystallization of this protein racemate. Molecular-dynamics simulations starting from the structure of the Pin1 WW domain suggest that the crystal structure closely resembles the conformation of this domain in solution. The structural data presented here should provide a basis for further studies of this important model system.
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