Packing motifs as predictors of the propensity of antibody fragments to crystallize

Edmundson, Allen B.; DeWitt, C.R.; Goldsteen, Benjamin Z.; Ramsland, Paul A.

doi:10.1016/s0022-0248(98)00820-3

Cited by 7 publications

(1 citation statement)

References 17 publications

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“…In this review, we will discuss the structures of the last two ß-strands, designated F (3-2) and G (3-3), and the turn, connecting these strands. The F-to-G loop is the most solvent exposed region of CL and CH1 domains of an Fab and its structure has been observed to vary for different isotypes of L and H chains [36]. For example, in Ï-chains the F-to-G loop forms a classical ß-hairpin structure, while in Î-chains the turn connecting the two ß-strands is expanded by two additional residues and a proline residue.…”

Section: General Features Of Immunoglobulin V and C Domainsmentioning

confidence: 99%

Incorporation of Long CDR3s into V Domains: Implications for the Structural Evolution of the Antibody-Combining Site

Ramsland

Kaushik

Marchalonis

et al. 2001

Exp Clin Immunogenet

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Available data suggest that ‘primitive’ antibody-combining sites often include longer than average HCDR3s. Long HCDR3 sequences have been reported in diverse vertebrates, including humans, cattle, camels and sharks. These long HCDR3 segments contain unusual sequence features such as stretches of Gly or Pro residues and multiple Cys residues. We examined how longer than average HCDR3s were accommodated in the V domains of human, murine and camel antibodies with known three-dimensional structures. The main conclusions were that (1) HCDR3s longer than 12 residues should protrude outward from the V domains; (2) descending HCDR3 polypeptides may utilize VL (including LCDR3) constituents as a platform, supporting the protruding segments; (3) intra- and inter-HCDR disulfides are frequently formed to rigidify the structure of HCDR3 or the combining site, and (4) V and C domains were possibly more similar in primordial antibodies than they are in their present day counterparts.

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Section: General Features Of Immunoglobulin V and C Domainsmentioning

confidence: 99%