Solution structures of the first and fourth TSR domains of F-spondin.
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.
Pääkkönen
Kimmo
K
Tatsuo Miyazawa Memorial Program, RIKEN Genomic Sciences Center, Yokohama, Japan.
Tossavainen
Helena
H
Permi
Perttu
P
Rakkolainen
Harri
H
Rauvala
Heikki
H
Raulo
Erkki
E
Kilpeläinen
Ilkka
I
Güntert
Peter
P
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D036341:Intercellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D051381:Rats; D016415:Sequence Alignment
D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; C498955:Spon1 protein, rat