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Functional annotation strategy for protein structures BACK TO CONTENTS PDF PREVIOUS NEXT
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Title

 

 

 

 

Functional annotation strategy for protein structures

 

Authors

Olivia Doppelt1, 2, Fabrice Moriaud2, Aur�lie Bornot1 & Alexandre G. de Brevern1*

 

Affiliation

1 Equipe de Bioinformatique G�nomique et Mol�culaire (EBGM), INSERM UMR-S 726, Universit� Denis Diderot - Paris 7, case 7113, 2, place Jussieu, 75251 Paris, France; 2 MEDIT SA, 2 rue du Belv�d�re, 91120, Palaiseau, France

 

Email

alexandre.debrevern@ebgm.jussieu.fr

 

Phone

(33) 1 44 27 77 31;

 

Fax

(33) 1 43 26 38 30; * Corresponding author

 

Article Type

Views & Challenges

 

Date

received January 26, 2007; revised March 14, 2006; accepted March 14, 2006; published online March 15, 2007

 

Abstract

Whole-genome sequencing projects are a major source of unknown function proteins. However, as predicting protein function from sequence remains a difficult task, research groups recently started to use 3D protein structures and structural models to bypass it. MED-SuMo compares protein surfaces analyzing the composition and spatial distribution of specific chemical groups (hydrogen bond donor, acceptor, positive, negative, aromatic, hydrophobic, guanidinium, hydroxyl, acyl and glycine). It is able to recognize proteins that have similar binding sites and thus, may perform similar functions. We present here a fine example which points out the interest of MED-SuMo approach for functional structural annotation.

 

Keywords

annotation; function; protein structures; prediction

 

Citation

Doppelt et al., Bioinformation 1(9): 357-359 (2007)

 

Edited by

B. Offmann

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

Copyright

Publisher

 

Copyright Transfer Agreement

The authors of published articles in Bioinformation automatically transfer the copyright to the publisher upon formal acceptance. However, the authors reserve right to use the information contained in the article for non commercial purposes.

 

License

This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.