members
carmela garcia-doval - doctoral student (fpu fellowship)
abhimanyu kumar singh - doctoral student (la caixa fellowship)
meritxell granell-puig - postdoc (juan de la cierva contract)
laura cordoba-garcia - postdoc
laura diaz-saez - undergraduate student
mariano marletta-vazquez - visiting technician
mark j van raaij - cientifico titular
Some viruses and bacteriophages attach to their host cell via proteins integral to their capsids, for example poliovirus, coxsackievirus and rhinovirus ('common cold virus'). Other viruses bind to their host cell receptors via specialised spike proteins (for example HIV, the AIDS-virus), or via specialised fibre proteins, like adenovirus, reovirus and the T-even bacteriophages.
The adenovirus fibre, the T4 short fibre and the reovirus sigmaC and sigma1 proteins have the same basic architecture: they are all trimeric and contain an N-terminal virus or bacteriophage attachment domain, a long, thin, but stable shaft domain and a more globular C-terminal cell attachment domain. In detail, they are more different: the adenovirus and T4-fibres are mainly composed of beta-sheet structure, the reovirus sigma1 and sigmaC proteins contain mainly alpha-helix.
These trimeric, fibrous proteins are very stable to denaturation by temperature or detergents. Our goal is to determine the structures of these proteins and thus to make an extensive inventory of stable trimeric folds present in nature. We also want to explain how different structural elements can lead to functionally similar proteins.
structure gallery
bacteriophage fibres
modification of bacteriophages
adenovirus fibres
collaborators
contact
webpage @ CNB, CSIC
positions