Solution structures of the first and fourth TSR domains of F-spondin

Kimmo Pääkkönen, Helena Tossavainen, Perttu Permi, Harri Rakkolainen, Heikki Rauvala, Erkki Raulo, Ilkka Kilpeläinen, Peter Guntert

    Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review


    F-spondin is a protein mainly associated with neuronal development. It attaches to the extracellular matrix and acts in the axon guidance of the developing nervous system. F-spondin consists of eight domains, six of which are TSR domains. The TSR domain family binds a wide range of targets. Here we present the NAIR solution structures of TSR1 and TSR4. TSR domains have an unusual fold that is characterized by a long, non-globular shape, consisting of two P-strands and one irregular extended strand. Three disulfide bridges and stack of alternating tryptophan and arginine side-chains stabilize the structure. TSR1 and TSR4 structures are similar to each other and to the previously determined TSR domain X-ray structures from another protein, TSP, although TSR4 exhibits a mobile loop not seen in other structures.
    TidskriftProteins : structure, function, and genetics
    Sidor (från-till)665-672
    Antal sidor8
    StatusPublicerad - 2006
    MoE-publikationstypA1 Tidskriftsartikel-refererad


    • 311 Basmedicin
    • 118 Biovetenskaper
    • 515 Psykologi

    Citera det här