ArticleBiomolecules2014
Similar structures to the E-to-H helix unit in the globin-like fold are found in other helical folds.
Article in Biomolecules, 2014. 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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5 citing papers in PubMed, 11 citations in OpenAlex.
- Conserved structural topologies in RNase A-like and trypsin-like serine proteases: a sequence-based folding analysis.BMC molecular and cell biology · 2025Article
- Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding.Molecules (Basel, Switzerland) · 2023Review
- Decoding an Amino Acid Sequence to Extract Information on Protein Folding.Molecules (Basel, Switzerland) · 2022Review
- Analyses of the folding sites of irregular β-trefoil fold proteins through sequence-based techniques and Gō-model simulations.BMC molecular and cell biology · 2020Article
- A new technique for predicting intrinsically disordered regions based on average distance map constructed with inter-residue average distance statistics.BMC structural biology · 2019Article
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4 authors at 1 institution in 1 country.
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Abstract
A protein in the globin-like fold contains six alpha-helices, A, B, E, F, G and H. Among them, the E-to-H helix unit (E, F, G and H helices) forms a compact structure. In this study, we searched similar structures to the E-to-H helix of leghomoglobin in the whole protein structure space using the Dali program. Several similar structures were found in other helical folds, such as KaiA/RbsU domain and Type III secretion system domain. These observations suggest that the E-to-H helix unit may be a common subunit in the whole protein 3D structure space. In addition, the common conserved hydrophobic residues were found among the similar structures to the E-to-H helix unit. Hydrophobic interactions between the conserved residues may stabilize the 3D structures of the unit. We also predicted the possible compact regions of the units using the average distance method.
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