Open AccessThe LCCL module
Author(s) -
Trexler Mária,
Bányai László,
Patthy László
Publication year - 2000
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2000.01641.x
Subject(s) - recombinant dna , domain (mathematical analysis) , chemistry , protein domain , biophysics , circular dichroism , limulus , biology , crystallography , biochemistry , gene , mathematical analysis , mathematics , paleontology
Here we show that Lgl1 protein, cub‐1‐related proteins, coch‐5b2‐related proteins, coagulation factor C of horse‐shoe crab and a predicted protein of Plasmodium falciparum share a homologous domain. Since this domain‐type was first identified in Limulus factor C, Coch‐5b2 and Lgl1 we propose the name LCCL for this domain‐family. The LCCL module of coch‐5b2 is of special biological interest because it has been shown recently that mutations affecting this module cause the deafness disorder DFNA9 in humans. With a view to defining the structure and function of the LCCL domain of human coch‐5b2 protein, we have expressed it in Escherichia coli and subjected it to preliminary structural characterization. Structure prediction and circular dichroism studies on the recombinant protein indicate that the domain possesses both α helices and β strands. It is shown that the mutations which cause hearing loss in humans affect residues that are critical for the integrity of the LCCL module of the coch‐5b2 protein.