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. 2002 Mar 19;99(7):4337–4342. doi: 10.1073/pnas.072557199

Figure 1.

Figure 1

Cartoon showing structure of the LDLR and mutant forms of the protein. (A) Full-length LDLR is depicted along with relevant protein domains. An arrow indicates the relative position of the naturally occurring mutation that created a transport defective LDLR. The mutation is a single amino acid substitution at amino acid position 544 (Gly-544–Val). (B) The truncated LDLR is depicted with a carboxyl-terminal KDEL ER retention signal. This receptor consists of the ligand-binding domains and is truncated at amino acid 354 before addition of KDEL. A single amino acid substitution was introduced at amino acid position 140 (Ile-140–Asp; arrow) to create a nonbinding form of the receptor.