ω-Turn: a novel β-turn mimic in globular proteins stabilized by main-chain to side-chain C−H···O interaction.
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
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| Title |
ω-Turn: a novel β-turn mimic in globular proteins stabilized by main-chain to side-chain C−H···O interaction.
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| Creator |
Dhar, Jesmita
Chakrabarti, Pinak Saini, Harpreet Raghava, G.P.S. Kishore, Raghuvansh |
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| Subject |
QR Microbiology
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| Description |
Mimicry of structural motifs is a common feature in proteins. The 10-membered hydrogen-bonded ring involving the main-chain C − O in a β-turn can be formed using a side-chain carbonyl group leading to Asx-turn. We show that the N − H component of hydrogen bond can be replaced by a C(γ) -H group in the side chain, culminating in a nonconventional C − H···O interaction. Because of its shape this β-turn mimic is designated as ω-turn, which is found to occur ∼ three times per 100 residues. Three residues (i to i + 2) constitute the turn with the C − H···O interaction occurring between the terminal residues, constraining the torsion angles ϕi + 1, ψi + 1, ϕi + 2 and χ'1(i + 2) (using the interacting C(γ) atom). Based on these angles there are two types of ω-turns, each of which can be further divided into two groups. C(β) -branched side-chains, and Met and Gln have high propensities to occur at i + 2; for the last two residues the carbonyl oxygen may participate in an additional interaction involving the S and amino group, respectively. With Cys occupying the i + 1 position, such turns are found in the metal-binding sites. N-linked glycosylation occurs at the consensus pattern Asn-Xaa-Ser/Thr; with Thr at i + 2, the sequence can adopt the secondary structure of a ω-turn, which may be the recognition site for protein modification. Location between two β-strands is the most common occurrence in protein tertiary structure, and being generally exposed ω-turn may constitute the antigenic determinant site. It is a stable scaffold and may be used in protein engineering and peptide design.
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| Publisher |
Wiley
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| Date |
2015-02
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| Type |
Article
PeerReviewed |
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| Relation |
http://onlinelibrary.wiley.com/doi/10.1002/prot.24720/abstract
http://crdd.osdd.net/open/1828/ |
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| Identifier |
Dhar, Jesmita and Chakrabarti, Pinak and Saini, Harpreet and Raghava, G.P.S. and Kishore, Raghuvansh (2015) ω-Turn: a novel β-turn mimic in globular proteins stabilized by main-chain to side-chain C−H···O interaction. Proteins, 83 (2). pp. 203-14. ISSN 1097-0134
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