Title : Solution structure and sugar-binding mechanism of mouse
latrophilin-1 RBL: a
7TM receptor-attached lectin-like
domain
Abstract :
- Latrophilin-1 ( Lat-1 ), a target receptor for alpha-Latrotoxin, is a putative G protein-coupled receptor implicated in synaptic function
- The extracellular portion of Lat-1 contains a rhamnose binding lectin (RBL)-like domain of unknown structure
- RBL domains , first isolated from the eggs of marine species, are also found in the ectodomains of other metazoan transmembrane proteins , including a recently discovered coreceptor of the neuronal axon guidance molecule SLT-1 /Slit
- Here, we describe a structure of this domain from the mouse Lat-1
- RBL adopts a unique alpha/beta fold with long structured loops important for monosaccharide recognition, as shown in the structure of a complex with L-rhamnose
- Sequence alignments and mutagenesis show that residues important for carbohydrate binding are often absent in other receptor-attached examples of RBL, including the SLT-1 /Slit coreceptor
- We postulate that this domain class facilitates direct protein-protein interactions in many transmembrane receptors
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
- 0. 7TM, domain
- 0. receptor, domain
- 3. proteins, domains
- 3. proteins, ectodomains
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):