The Global Sequence Signature algorithm unveils a structural network surrounding heavy chain CDR3 loop in Camelidae variable domains

• Published in: Biochimica et biophysica acta Vol. 1830; no. 6; pp. 3373 - 3381
• Main Authors: Kastelic, Damjana, Soler, Nicolas, Komel, Radovan, Pompon, Denis
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.06.2013; Elsevier
• Subjects: Algorithms; Animals; antibodies; antigens; Camelidae; Camelidae variable domain; Camelids, New World - genetics; Camelids, New World - immunology; camels; Camelus - genetics; Camelus - immunology; Chemical and Process Engineering; Co-evolution; Complementarity determining region 3 (CDR3); Complementarity Determining Regions - genetics; Complementarity Determining Regions - immunology; Engineering Sciences; Food engineering; Immunoglobulin Heavy Chains - genetics; Immunoglobulin Heavy Chains - immunology; Life Sciences; llamas; maturation; Multiple sequence alignment; protein engineering; Protein Structure, Secondary; Sequence Alignment - methods; Sequence Analysis, Protein - methods; VHH; Multiple sequence alignment; GSS; FR; Camelidae variable domain; Complementarity determining region 3 (CDR3); PCA; CDR; SCA; VH; VL; VHH; MSA; Co-evolution; MDS; Ig; CONTACTS; ALLOSTERIC COMMUNICATION; ANTIBODY FRAGMENT; CRYSTAL-STRUCTURE; IMMUNOGLOBULINS; PREDICTION; V-H; CORRELATED MUTATIONS; PROTEINS; RESIDUES; LIGHT-CHAINS

A large fraction of camelid (camels and llamas) antibodies is composed of heavy chain-only homodimers, able to recognise antigens with their variable domain. Events in somatic assembly and maturation of antibodies such as hypermutations and rearrangement of variable loops (CDRs — complementary deter...