Anna Tramontano: The computational analysis of macromolecular interactions: The case of antibodies [Departmental Colloquium]

Professor Anna Tramontano from Sapienza University of Rome, Italy is giving this talk.

Anna Tramontano

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Abstract

The computational analysis of macromolecular interactions: The case of antibodies

Anna Tramontano - Physics Department - Sapienza University of Rome (I)

Antibodies or immunoglobulins are fascinating molecules from both a functional and structural point of view. They have the ability to recognize virtually any foreign molecule with exquisite specificity and very high affinity. These properties are brought about by their 3D architecture, which consists of a tetramer of two identical pairs of polypeptide chains: the heavy and light chains. Each chain includes homologous domains that have a similar tertiary structure to each other. With few exceptions, two domains are present in the light chain—one variable and one constant—and four or more domains are present in the heavy chain—one variable and three or more that are constant. The two N-terminal domains of the polypeptide chains are called variable domains (VL and VH, respectively), and they are responsible for antigen binding.
I will discuss our protocol for inferring the structure of antibodies from their sequences, for predicting which residues are in contact with the antigen and how this can be exploited to speed up the antibody humanization process.
I will also briefly discuss how the predicted structure of the antigen-binding site can be used to classify antibodies found in cohorts of patients with diseases characterized by a clonal expansion of neoplastic mature B lymphocytes and how this classification might correlate with the pathological phenotype and the disease prognosis.
 

 

 

Published Aug. 22, 2014 11:25 AM - Last modified Oct. 31, 2014 9:52 AM