Protein-protein recognition and the association of immunoglobulin constant domains.
Four immunoglobulin constant domain interfaces were analysed to determine how the light and heavy chains of the domains recognize each other and secondarily, why the packing of the beta sheets is different from that normally observed in the interior of domains of beta sheet proteins. It was found that two bulky groups in the centre of each of the domain interfaces prevent the alignment of sheet axes by intercalating with residues in the sheet opposite. This intercalation forms the basis of constant domain light chain-heavy chain recognition.
Miller
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European Molecular Biology Laboratory, Heidelberg, F.R.G.
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D006860:Hydrogen Bonding; D007127:Immunoglobulin Constant Regions / Q000737:chemistry / Q000378:metabolism*; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry / Q000378:metabolism*; D007147:Immunoglobulin Light Chains / Q000737:chemistry / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011228:Prealbumin / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014867:Water
D007127:Immunoglobulin Constant Regions; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D011228:Prealbumin; D014867:Water