Structural biology. LDL receptor's beta-propeller displaces LDL.
Innerarity
Thomas L
TL
Gladstone Institute of Cardiovascular Disease, San Francisco, CA 94110, USA. tinnerarity@gladstone.ucsf.edu
D000595:Amino Acid Sequence; D053299:Apolipoprotein B-100; D001055:Apolipoproteins B / Q000378:metabolism; D001057:Apolipoproteins E / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D018360:Crystallography, X-Ray; D011992:Endosomes / Q000378:metabolism*; D004815:Epidermal Growth Factor / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008077:Lipoproteins, LDL / Q000378:metabolism*; D008247:Lysosomes / Q000378:metabolism; D008954:Models, Biological; D011485:Protein Binding; D011498:Protein Precursors / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011973:Receptors, LDL / Q000737:chemistry* / Q000378:metabolism*; D020449:Repetitive Sequences, Amino Acid
D053299:Apolipoprotein B-100; D001055:Apolipoproteins B; D001057:Apolipoproteins E; D008024:Ligands; D008077:Lipoproteins, LDL; D011498:Protein Precursors; D011973:Receptors, LDL; D004815:Epidermal Growth Factor