In:
Journal of Bioinformatics and Computational Biology, World Scientific Pub Co Pte Ltd, Vol. 04, No. 02 ( 2006-04), p. 415-424
Abstract:
The third complementary determining region of the immunoglobulin heavy chain (CDR H3) is one of the more difficult structures to model due to genetic reasons. However, the conformation of proximal to β-framework ("torso") part of the CDR H3 is very predictable. Current "CDR's canonical classes" theory is based on identifying the key positions, H94 and H101. We can determine the CDR H3 "torso" structure if arginine or lysine is present in the H94 position and/or aspartic acid in the H101 position. We target the case characterized by the absence of key residues in both the H94 and H101 positions. There has not been discussion on this case in the literature. 51 CDR H3 structures of this nature are analyzed and we established new sequence-structure rules. These rules contribute to more accurate modeling of the antibody's structure.
Type of Medium:
Online Resource
ISSN:
0219-7200
,
1757-6334
DOI:
10.1142/S0219720006001874
Language:
English
Publisher:
World Scientific Pub Co Pte Ltd
Publication Date:
2006
SSG:
12
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