Details of the Target
General Information of Target
Target ID | LDTP14558 | |||||
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Target Name | Immunoglobulin kappa variable 3-15 (IGKV3-15) | |||||
Gene Name | IGKV3-15 | |||||
Synonyms |
Immunoglobulin kappa variable 3-15; Ig kappa chain V-III region CLL; Ig kappa chain V-III region POM |
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3D Structure | ||||||
Sequence |
MRLPAQLLGLLMLWVPGSSEDIVMTQTPLSLPVTPGEPASISCRSSQSLLDSDDGNTYLD
WYLQKPGQSPQLLIYTLSYRASGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQRIEF P |
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Target Bioclass |
Immunoglobulin
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Subcellular location |
Secreted
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Function |
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
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Uniprot ID | ||||||
Ensemble ID | ||||||
HGNC ID |
Probe(s) Labeling This Target
ABPP Probe
Probe name | Structure | Binding Site(Ratio) | Interaction ID | Ref | |
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DBIA Probe Info |
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C46(0.80) | LDD3370 | [1] |
Competitor(s) Related to This Target