Evolutionary and structural influences on light chain constant (CL) region of human and mouse immunoglobulins.
A comparison of five constant region sequences of human and mouse k and lambda immunoglobulin chains has been undertaken in order to reveal sequence homologies and evolutionary relationships. Simultaneously, a comparison with the three-dimensional structure of one mouse k-chain (McPC 603) has suggested structural reasons why many of the residues are invariant or conserved along k versus lambda lines. There are a number of residues that have remained invariant despite exposed positions for reasons that do not apppear to be connected with the folding of the CL domain.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001536:Bence Jones Protein; D005075:Biological Evolution; D006801:Humans; D007140:Immunoglobulin Fab Fragments; D007147:Immunoglobulin Light Chains / Q000096:biosynthesis; D007145:Immunoglobulin kappa-Chains; D007146:Immunoglobulin lambda-Chains; D051379:Mice; D011487:Protein Conformation; D013045:Species Specificity; D014961:X-Ray Diffraction
D000596:Amino Acids; D007140:Immunoglobulin Fab Fragments; D007147:Immunoglobulin Light Chains; D007145:Immunoglobulin kappa-Chains; D007146:Immunoglobulin lambda-Chains; D001536:Bence Jones Protein