Global analysis of VHHs framework regions with a structural alphabet / Floriane Noël  

Public ISBD Faire une suggestion d'achat Titre : Global analysis of VHHs framework regions with a structural alphabet Type de document : document électronique Auteurs : Floriane Noël, Auteur ; Alain Malpertuy, Auteur ; Alexandre De Brevern, Auteur Editeur : Elsevier Année de publication : 2016 Importance : Volume 131, Pages 11-19 Langues : Anglais (eng) Catégories : 572 Biochimie Tags : 'Secondary structure  Sequence structure relationship  Structural alphabet  Antibodies  Frameworks  Quantitative Methods (q-bio.QM)  Biomolecules (q-bio.BM)'. Index. décimale : 572 Résumé : The VHHs are antigen-binding region/domain of camelid heavy chain antibodies (HCAb). They have many interesting biotechnological and biomedical properties due to their small size, high solubility and stability, and high affinity and specificity for their antigens. HCAb and classical IgGs are evolutionary related and share a common fold. VHHs are composed of regions considered as constant, called the frameworks (FRs) connected by Complementarity Determining Regions (CDRs), a highly variable region that provide interaction with the epitope. Actually, no systematic structural analyses had been performed on VHH structures despite a significant number of structures. This work is the first study to analyse the structural diversity of FRs of VHHs. Using a structural alphabet that allows approximating the local conformation, we show that each of the four FRs do not have a unique structure but exhibit many structural variant patterns. Moreover, no direct simple link between the local conformational change and amino acid composition can be detected. These results indicate that long-range interactions affect the local conformation of FRs and impact the building of structural models. En ligne : https://arxiv.org/abs/1610.01391 Format de la ressource électronique : PDF Global analysis of VHHs framework regions with a structural alphabet [document électronique] / Floriane Noël, Auteur ; Alain Malpertuy, Auteur ; Alexandre De Brevern, Auteur . - Elsevier, 2016 . - Volume 131, Pages 11-19. Langues : Anglais (eng) Catégories : 572 Biochimie Tags : 'Secondary structure  Sequence structure relationship  Structural alphabet  Antibodies  Frameworks  Quantitative Methods (q-bio.QM)  Biomolecules (q-bio.BM)'. Index. décimale : 572 Résumé : The VHHs are antigen-binding region/domain of camelid heavy chain antibodies (HCAb). They have many interesting biotechnological and biomedical properties due to their small size, high solubility and stability, and high affinity and specificity for their antigens. HCAb and classical IgGs are evolutionary related and share a common fold. VHHs are composed of regions considered as constant, called the frameworks (FRs) connected by Complementarity Determining Regions (CDRs), a highly variable region that provide interaction with the epitope. Actually, no systematic structural analyses had been performed on VHH structures despite a significant number of structures. This work is the first study to analyse the structural diversity of FRs of VHHs. Using a structural alphabet that allows approximating the local conformation, we show that each of the four FRs do not have a unique structure but exhibit many structural variant patterns. Moreover, no direct simple link between the local conformational change and amino acid composition can be detected. These results indicate that long-range interactions affect the local conformation of FRs and impact the building of structural models. En ligne : https://arxiv.org/abs/1610.01391 Format de la ressource électronique : PDF

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