Antibody elbow angles are influenced by their light chain class

Journal Article · Thu Jan 12 00:00:00 EST 2006 · Journal of Molecular Biology, vol. 357, no. 5, April 14, 2006, pp. 1566-1574

DOI:https://doi.org/10.1016/j.jmb.2006.01.023· OSTI ID:898021

Stanfield, R; Zemla, A; Wilson, I; Rupp, B

We have examined the elbow angles for 365 different Fab fragments, and observe that Fabs with lambda light chains have adopted a wider range of elbow angles than their kappa-chain counterparts, and that the lambda light chain Fabs are frequently found with very large (>195{sup o}) elbow angles. This apparent hyperflexibility of lambda-chain Fabs may be due to an insertion in their switch region, which is one residue longer than in kappa chains, with glycine occurring most frequently at the insertion position. A new, web-based computer program that was used to calculate the Fab elbow angles is also described.

• Research Organization: Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
• Sponsoring Organization: USDOE
• DOE Contract Number: W-7405-ENG-48
• OSTI ID: 898021
• Report Number(s): UCRL-JRNL-218128; TRN: US200706%%199
• Journal Information: Journal of Molecular Biology, vol. 357, no. 5, April 14, 2006, pp. 1566-1574, Journal Name: Journal of Molecular Biology, vol. 357, no. 5, April 14, 2006, pp. 1566-1574
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
COMPUTER CODES
GLYCINE
RESIDUES