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| Functional annotation strategy for protein structures
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Authors | Olivia Doppelt1, 2, Fabrice Moriaud2, Aur�lie Bornot1 & Alexandre G. de Brevern1*
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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
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| alexandre.debrevern@ebgm.jussieu.fr
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Phone | (33) 1 44 27 77 31;
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Fax | (33) 1 43 26 38 30; * Corresponding author
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Article Type | Views & Challenges
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Date | received January 26, 2007; revised March 14, 2006; accepted March 14, 2006; published online March 15, 2007
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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.
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Keywords | annotation; function; protein structures; prediction
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Citation | Doppelt et al., Bioinformation 1(9): 357-359 (2007)
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Edited by | B. Offmann
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ISSN | 0973-2063
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Publisher |
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Copyright | Publisher
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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.
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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.
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