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...

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Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2006-08, Vol.64 (3), p.665-672
Main Authors: Pääkkönen, Kimmo, Tossavainen, Helena, Permi, Perttu, Rakkolainen, Harri, Rauvala, Heikki, Raulo, Erkki, Kilpeläinen, Ilkka, Güntert, Peter
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Crystallography, X-Ray
extracellular matrix
F-spondin
Magnetic Resonance Spectroscopy - methods
Molecular Sequence Data
neuron development
NMR structure
Peptides - chemistry
Peptides - genetics
Protein Structure, Tertiary
Rats
Sequence Alignment
TSR
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Summary: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 β‐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. Proteins 2006. © 2006 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.21030