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

Proteins. 2006 Aug 15;64(3):665-72. doi: 10.1002/prot.21030.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Intercellular Signaling Peptides and Proteins
  • Magnetic Resonance Spectroscopy / methods
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / genetics
  • Protein Structure, Tertiary*
  • Rats
  • Sequence Alignment

Substances

  • Intercellular Signaling Peptides and Proteins
  • Peptides
  • Sponf protein, rat