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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Bibliographic Details
Published in:	Proteins, structure, function, and bioinformatics Vol. 64; no. 3; pp. 665 - 672
Main Authors:	Pääkkönen, Kimmo, Tossavainen, Helena, Permi, Perttu, Rakkolainen, Harri, Rauvala, Heikki, Raulo, Erkki, Kilpeläinen, Ilkka, Güntert, Peter
Format:	Journal Article
Language:	English
Published:	Hoboken Wiley Subscription Services, Inc., A Wiley Company 15-08-2006
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.
Bibliography:	ark:/67375/WNG-FR9VHF5P-2 ArticleID:PROT21030 istex:8A058FD28EE5D8C6DC03D0F8084BBF4FA9AB7DD5 These authors contributed equally to this work. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0887-3585 1097-0134
DOI:	10.1002/prot.21030