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Research article summary (published 19 Aug 2009):

Protein sectors: evolutionary units of three-dimensional structure.

Full Abstract

Proteins display a hierarchy of structural features at primary, secondary, tertiary, and higher-order levels, an organization that guides our current understanding of their biological properties and evolutionary origins. Here, we reveal a structural organization distinct from this traditional hierarchy by statistical analysis of correlated evolution between amino acids. Applied to the S1A serine proteases, the analysis indicates a decomposition of the protein into three quasi-independent groups of correlated amino acids that we term "protein sectors." Each sector is physically connected in the tertiary structure, has a distinct functional role, and constitutes an independent mode of sequence divergence in the protein family. Functionally relevant sectors are evident in other protein families as well, suggesting that they may be general features of proteins. We propose that sectors represent a structural organization of proteins that reflects their evolutionary histories.

 

Author information

Author/s: Halabi, Najeeb (N); Rivoire, Olivier (O); Leibler, Stanislas (S); Ranganathan, Rama (R);

Affiliation: Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, USA.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Cell (Cell), published in United States. (Language: eng)

Reference: 2009-Aug; vol 138 (issue 4) : pp 774-86

Dates: Created 2009/08/25; Completed 2009/09/23;

PMID: 19703402, status: MEDLINE (last retrieval date: 9/23/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Associated Chemicals: Amino Acids (0) ; Serine Endopeptidases (EC 3.4.21.-)

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