9eag

The Structure of ApoB100 from Human Low-Density Lipoprotein

spinqualitylabelsall models 9eag, resolution 9.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9eag is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease APOB_HUMAN Homozygous familial hypercholesterolemia. The disease is caused by variants affecting the gene represented in this entry. Most cases of FHBL1 result from nonsense mutations in the APOB gene that lead to a premature stop codon, which generate prematurely truncated apo B protein products (PubMed:21981844). The disease is caused by variants affecting the gene represented in this entry. Defects in APOB associated with defects in other genes (polygenic) can contribute to hypocholesterolemia. Function APOB_HUMAN Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor.

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