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

    Research output: Contribution to journalArticleScientificpeer-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.
    Original languageEnglish
    JournalProteins : structure, function, and genetics
    Issue number3
    Pages (from-to)665-672
    Number of pages8
    Publication statusPublished - 2006
    MoE publication typeA1 Journal article-refereed

    Fields of Science

    • 311 Basic medicine
    • 118 Biological sciences
    • 515 Psychology

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