A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn

V. S. Ananthanarayanan; K. V. Soman; C. Ramakrishnan

doi:10.1016/0022-2836(87)90211-7

A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn

V. S. Ananthanarayanan, K. V. Soman, C. Ramakrishnan

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a β-turn is seen in several synthetic peptides and has been suggested to be the conformational requirement for proline hydroxylation in nascent procollagen. Using a simple algorithm for detecting secondary structures, we have analysed crystal structure data on 40 globular proteins and have found eight examples of the collagen-helix + β-turn supersecondary structure in 15 proteins that contain the collagen-like helical segments.

Original language	English (US)
Pages (from-to)	705-709
Number of pages	5
Journal	Journal of Molecular Biology
Volume	198
Issue number	4
DOIs	https://doi.org/10.1016/0022-2836(87)90211-7
State	Published - Dec 20 1987
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Biophysics
Structural Biology

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10.1016/0022-2836(87)90211-7

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abstract = "A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a β-turn is seen in several synthetic peptides and has been suggested to be the conformational requirement for proline hydroxylation in nascent procollagen. Using a simple algorithm for detecting secondary structures, we have analysed crystal structure data on 40 globular proteins and have found eight examples of the collagen-helix + β-turn supersecondary structure in 15 proteins that contain the collagen-like helical segments.",

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AB - A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a β-turn is seen in several synthetic peptides and has been suggested to be the conformational requirement for proline hydroxylation in nascent procollagen. Using a simple algorithm for detecting secondary structures, we have analysed crystal structure data on 40 globular proteins and have found eight examples of the collagen-helix + β-turn supersecondary structure in 15 proteins that contain the collagen-like helical segments.

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A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn

Abstract

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