Evolutionary and structural influences on light chain constant (CL) region of human and mouse immunoglobulins. | Zendy

Elvin A. Kabat | Zendy; Eduardo A. Padlan | Zendy; D. Rhodri Davies | Zendy

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Evolutionary and structural influences on light chain constant (CL) region of human and mouse immunoglobulins.

Author(s) -

Elvin A. Kabat,

Eduardo A. Padlan,

D. Rhodri Davies

Publication year - 1975

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.72.7.2785

Subject(s) - immunoglobulin light chain , lambda , invariant (physics) , antibody , folding (dsp implementation) , biology , constant (computer programming) , evolutionary biology , polypeptide chain , genetics , computational biology , protein folding , amino acid , biochemistry , mathematics , physics , computer science , electrical engineering , optics , mathematical physics , programming language , engineering

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.

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