Publication Abstract from PubMed
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 NMR solution structures of TSR1 and TSR4. TSR domains have an unusual fold that is characterized by a long, nonglobular shape, consisting of two beta-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.
Solution structures of the first and fourth TSR domains of F-spondin.,Paakkonen K, Tossavainen H, Permi P, Rakkolainen H, Rauvala H, Raulo E, Kilpelainen I, Guntert P Proteins. 2006 Aug 15;64(3):665-72. PMID:16736493[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
