1VEX
F-spondin TSR domain 4
Summary for 1VEX
| Entry DOI | 10.2210/pdb1vex/pdb |
| NMR Information | BMRB: 10002 |
| Descriptor | F-spondin (1 entity in total) |
| Functional Keywords | f-spondin, tsr, cell adhesion |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Secreted, extracellular space, extracellular matrix: P35446 |
| Total number of polymer chains | 1 |
| Total formula weight | 6240.19 |
| Authors | Paakkonen, K.,Tossavainen, H.,Permi, P.,Kilpelainen, I.,Guntert, P. (deposition date: 2004-04-06, release date: 2005-04-19, Last modification date: 2023-12-27) |
| Primary citation | 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, 64:665-672, 2006 Cited by PubMed 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. PubMed: 16736493DOI: 10.1002/prot.21030 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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