Published: 24 July, 2025 | Volume 9 - Issue 1 | Pages: 001-012
Figure 2:
Courtesy ref no-51The structure of lipoprotein lipase (LPL) homodimer and LPL–LPL-LPL-LPL-LPL-glycosylphosphatidylinositol-anchored high‐density lipoprotein binding protein 1 (GPIHBP1) complex. (a) N‐terminal hydrolase with Lid domain and C‐terminal domain with lipid‐binding loop of LPL. Signal peptide (SP) and N‐glycosylation sites (N70 and N386) are shown. (b) Acidic domain and cysteine‐rich LU (Ly6/uPAR) domain, and C‐terminal hydrophobic regions of GPI‐anchored protein are shown. Y38 is modified by sulfation, and N‐glycosylation site (N78) is shown. (c) Ribbon model structures of Bos taurus LPL homodimer are obtained from PDB ID: 8ERL at MMDB (NCBI). Head‐to‐tail homodimer formation was thought to be critical for LPL secretion and the maintenance of the enzymatic activity, whereas recent data suggested that LPL homodimer is present in vitro, and LPL is synthesized and secreted as a monomer in vivo. (d) Ribbon model structures of human LPL/GPIHBP1 complex (pink and brown) are obtained from PDB ID: 6E7K at MMDB (NCBI). N‐terminal LPL α/β‐hydrolase domain and C‐terminal PLAT (polycystin‐1, lipoxygenase, α‐toxin) domain of LPL and GPIHBP1 LU domain are shown. Portions of angiopoietin‐like protein (ANGPTL) binding site, the lid domain covering the catalytic active site, heparin binding sites, and Trp‐rich loop in LPL are also shown. N‐terminal sequences (residues 21–61) containing the disordered acidic domain of GPIHBP1 are not defined in the ribbon diagram.
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