Research Article
Isolation, Characterization, and Molecular Modeling of a Rheumatoid Factor from a Hepatitis C Virus Infected Patient with Sjögren’s Syndrome
Table 1
Comparison of contact residues in RF61 and RFL11 interaction with Fc.
| | | CDR residue | Fc contact | Fc chain | Types of contact | | | (IMGT numbering) |
| | | — | | | | H2 | Tyr52 (s) | Lys439 (s) | A | Hydrophobic | | | Ser440 (m) | A | H-bonding | | Tyr53 (s) | Gln438 (s) | A | H-bonding | | | Ser440 (s) | A | H-bonding | | Ser54 (s) | Gln438 (m) | A | H-bonding | | | | | | | | H3 | Asp98 (s) | Arg355 (s) | B | Ion interaction | | | Asp356 (s) | B | Anion-pi | | Tyr100 (s) | Thr350 (s) | A | H-bonding | | | Lys439 (s) | A | Cation-pi | | Thr100a (s) | Ser440 (m) | A | H-bonding | | | Arg355 (s) | B | H-bonding | | Asp100c (s) | Arg355 (s) | B | Ion interaction |
| | | | | | | H2 | Phe48 (s)* | Asp356 (s) | A | Anion-pi | | Tyr49 (s) | Asp356 (s) | A | H-bonding | | | Lys439 (s) | A | Cation-pi | | Arg50 (s) | Gln438 (s) | A | H-bonding | | | Tyr436 (s) | A | H-bonding | | Ser51 (s) | Gln438 (m) | A | H-bonding | | Asn52 (s)* | Gln438 (m) | A | H-bonding | | | | | | | | H3 | Thr102 (s)* | Ser444 (s) | A | H-bonding | | Thr103 (s)* | Ser442 (s) | A | H-bonding | | Asp104 (s)* | Arg355 (s) | A | Ion interaction | | Phe105 (s)* | Pro352 (s) | A | Hydrophobic | | | Pro352 (s) | B | Hydrophobic | | Tyr106 (s) | Arg355 (s) | A | Cation-pi | | Tyr107 (s) | Arg355 (s) | A | Cation-pi |
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Abbreviations: (s) and (m) denote the side chain and the main chain, respectively.
*Denotes the residue of somatic mutation.
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