Structural highlights
Function
[SPON1_RAT] Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Paakkonen K, Tossavainen H, Permi P, Rakkolainen H, Rauvala H, Raulo E, Kilpelainen I, Guntert P. Solution structures of the first and fourth TSR domains of F-spondin. Proteins. 2006 Aug 15;64(3):665-72. PMID:16736493 doi:http://dx.doi.org/10.1002/prot.21030
