1LE2

STRUCTURAL BASIS FOR ALTERED FUNCTION IN THE COMMON MUTANTS OF HUMAN APOLIPOPROTEIN-E

Summary for 1LE2

• Entry DOI: 10.2210/pdb1le2/pdb
• Descriptor: APOLIPOPROTEIN E2 (1 entity in total)
• Functional Keywords: lipoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02649
• Total number of polymer chains: 1
• Total formula weight: 16689.03

Authors

Wilson, C.,Agard, D.A. (deposition date: 1991-08-22, release date: 1992-10-15, Last modification date: 2024-02-14)

Primary citation

Wilson, C.,Mau, T.,Weisgraber, K.H.,Wardell, M.R.,Mahley, R.W.,Agard, D.A.
Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein.
Structure, 2:713-718, 1994

PubMed Abstract: Apolipoprotein-E (apo-E), a 34kDa blood plasma protein, plays a key role in directing cholesterol transport via its interaction with the low density lipoprotein (LDL) receptor. The amino-terminal domain of apo-E forms an unusually elongated four-helix bundle arranged such that key basic residues involved in LDL receptor binding form a cluster at the end of one of the helices. A common apo-E variant, apo-E2, corresponding to the single-site substitution Arg158-->Cys, displays minimal LDL receptor binding and is associated with significant changes in plasma cholesterol levels and increased risk of coronary heart disease. Surprisingly, the site of mutation in this variant is physically well removed (> 12A) from the cluster of LDL receptor binding residues.

PubMed: 7994571
DOI: 10.1016/S0969-2126(00)00072-1

Experimental method

X-RAY DIFFRACTION (3 Å)