A novel secondary structure based on fused five-membered rings motif.
DIR@IMTECH: CSIR-Institute of Microbial Technology
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Title |
A novel secondary structure based on fused five-membered rings motif.
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Creator |
Dhar, Jesmita
Kishore, Raghuvansh Chakrabarti, Pinak |
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Subject |
QR Microbiology
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Description |
An analysis of protein structures indicates the existence of a novel, fused five-membered rings motif, comprising of two residues (i and i + 1), stabilized by interresidue Ni+1-H∙∙∙Ni and intraresidue Ni+1-H∙∙∙O=Ci+1 hydrogen bonds. Fused-rings geometry is the common thread running through many commonly occurring motifs, such as β-turn, β-bulge, Asx-turn, Ser/Thr-turn, Schellman motif, and points to its structural robustness. A location close to the beginning of a β-strand is rather common for the motif. Devoid of side chain, Gly seems to be a key player in this motif, occurring at i, for which the backbone torsion angles cluster at ~(-90°, -10°) and (70°, 20°). The fused-rings structures, distant from each other in sequence, can hydrogen bond with each other, and the two segments aligned to each other in a parallel fashion, give rise to a novel secondary structure, topi, which is quite common in proteins, distinct from two major secondary structures, α-helix and β-sheet. Majority of the peptide segments making topi are identified as aggregation-prone and the residues tend to be conserved among homologous proteins.
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Publisher |
NPG
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Date |
2016
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Identifier |
http://crdd.osdd.net/open/1864/1/22.pdf
Dhar, Jesmita and Kishore, Raghuvansh and Chakrabarti, Pinak (2016) A novel secondary structure based on fused five-membered rings motif. Scientific reports, 6. p. 31483. ISSN 2045-2322 |
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Relation |
http://www.nature.com/articles/srep31483
http://crdd.osdd.net/open/1864/ |
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