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Background

Anaplastic Lymphoma Kinase (ALK) is a member of the family of Receptor Tyrosine Kinases (RTKs), a family of biomolecules that are primarily responsible for biosignaling pathways such as the insulin signaling pathway. It was discovered as a novel tyrosine phosphoprotein in 1994 in an analysis of Anaplastic Large-Cell Lymphoma, the protein's namesake. A full analysis and characterization of ALK was completed in 1997, properly identifying it as a RTK, and linking it closely to Leukocyte Tyrosine Kinase (LTK).

Structure

Domains

Three Helix Bundle-like Domain

The three helix bundle-like domain mainly has a structural function overall as it interacts with the tumor necrosis factor-like domain upon ligand binding.

Poly-Glycine Domain

Located between the three helix bundle-like domain and the tumor necrosis factor-like domain, the poly-glycine domain has an important structural role.

Tumor Necrosis Factor-like Domain

The tumor necrosis factor-like domain interacts with the three helix bundle-like domain to begin the conformational changes associated with ligand binding. The three helix bundle-like domain's α-helix interacts with the helix α-1' and β strand A-1'. This domain also assists in mediating ligand binding with the epidermal growth factor-like domain.

Epidermal Growth Factor-like Domain

The is very malleable and repositioning of this domain is essential for activation of the protein. This domain is able to undergo conformational changes with the ligand bound and when in contact with the tumor necrosis factor-like domain.

Binding Site

The binding site of Anaplastic Lymphoma Kinase is approximately from E859 to D1006 on one monomer. This site doesn't start out surrounding the ligand, instead the proximity of the ligand allows conformational changes across the protein.

Dimerization of Anaplastic Lymphoma Kinase

To achieve

Function

Disease

Relevance

Structural highlights

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