The dimerization interface of the glycoprotein Ibβ transmembrane domain corresponds to polar residues within a leucine zipper motif

Protein Science

Volumn 20, Issue 11, 2011, Pages 1814-1823

  Wei, Peng ^a   Liu, Xin ^b   Hu, Miao Hui ^a   Zuo, Li Min ^a   Kai, Ming ^b   Wang, Rui ^b   Luo, Shi Zhong ^a  

^a BEIJING UNIVERSITY OF CHEMICAL TECHNOLOGY   (China)

^b LANZHOU UNIVERSITY   (China)

Author keywords

Dimerization; GP Ib IX complex; Leucine zipper motif; Polar residues; TOXCAT; Transmembrane domain

Indexed keywords

ALANINE; DISULFIDE; GLYCOPROTEIN; GLYCOPROTEIN IB BETA; HOMODIMER; LEUCINE; THIOL; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; COMPUTER MODEL; DIMERIZATION; HYDROGEN BOND; LEUCINE ZIPPER MOTIF; MUTAGENESIS; MUTATION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN MOTIF; TRANSMEMBRANE DOMAIN;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CELL MEMBRANE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HYDROGEN BONDING; LEUCINE ZIPPERS; MODELS, MOLECULAR; MUTATION; PLATELET GLYCOPROTEIN GPIB-IX COMPLEX; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ANALYSIS, PROTEIN; STATIC ELECTRICITY;

ESCHERICHIA COLI;

EID: 80054729335     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.713     Document Type: Article

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