The LCCL module

Eur J Biochem. 2000 Sep;267(18):5751-7. doi: 10.1046/j.1432-1327.2000.01641.x.


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 alpha helices and beta 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blood Coagulation Factors / chemistry*
  • Blood Coagulation Factors / genetics
  • Chickens
  • Circular Dichroism
  • Databases, Factual
  • Deafness / genetics*
  • Exons
  • Extracellular Matrix Proteins
  • Humans
  • Mice
  • Molecular Sequence Data
  • Mutation
  • Plasmodium falciparum / chemistry
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Proteins / genetics
  • Rats
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Software


  • Blood Coagulation Factors
  • COCH protein, human
  • Coch protein, mouse
  • CrispId2 protein, rat
  • Extracellular Matrix Proteins
  • Proteins
  • Recombinant Proteins