Determination of Amino Acid Pairs Sensitive to Variants in Human Low-density Lipoprotein Receptor Precursor by Means of a Random Approach

2002 ◽  
Vol 6 (6) ◽  
pp. 401-406 ◽  
Author(s):  
Guang Wu ◽  
Shaomin Yan
Keyword(s):  
Amino Acid ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Low Density Lipoprotein Receptor ◽  
Density Lipoprotein Receptor ◽  
Random Approach

Influence of an asparagine to lysine mutation at amino acid 3516 of apolipoprotein B on low-density lipoprotein receptor binding

2002 ◽  
Vol 321 (1-2) ◽  
pp. 113-121 ◽  
Author(s):  
Dairena Gaffney ◽  
Clive R. Pullinger ◽  
Denis St.J. O'Reilly ◽  
Michael S. Hoffs ◽  
Isobel Cameron ◽  
...  
Keyword(s):  
Amino Acid ◽  
Receptor Binding ◽  
Apolipoprotein B ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Low Density Lipoprotein Receptor ◽  
Density Lipoprotein Receptor

scholarly journals Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor.

1988 ◽  
Vol 107 (6) ◽  
pp. 2749-2756 ◽  
Author(s):  
M E Durkin ◽  
S Chakravarti ◽  
B B Bartos ◽  
S H Liu ◽  
R L Friedman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Open Reading Frame ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Low Density Lipoprotein Receptor ◽  
Reading Frame ◽  
Density Lipoprotein Receptor

Entactin (nidogen), a 150-kD sulfated glycoprotein, is a major component of basement membranes and forms a highly stable noncovalent complex with laminin. The complete amino acid sequence of mouse entactin has been derived from sequencing of cDNA clones. The 5.9-kb cDNA contains a 3,735-bp open reading frame followed by a 3'-untranslated region of 2.2 kb. The open reading frame encodes a 1,245-residue polypeptide with an unglycosylated Mr of 136,500, a 28-residue signal peptide, two Asn-linked glycosylation sites, and two potential Ca2+-binding sites. Analysis of the deduced amino acid sequence predicts that the molecule consists of two globular domains of 70 and 36 kD separated by a cysteine-rich domain of 28 kD. The COOH-terminal globular domain shows homology to the EGF precursor and the low density lipoprotein receptor. Entactin contains six EGF-type cysteine-rich repeat units and one copy of a cysteine-repeat motif found in thyroglobulin. The Arg-Gly-Asp cell recognition sequence is present in one of the EGF-type repeats, and a synthetic peptide from the putative cell-binding site of entactin was found to promote the attachment of mouse mammary tumor cells.

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