Title : The structure of human 4F2hc ectodomain provides a model for homodimerization and electrostatic interaction with plasma membrane.

Pub. Date : 2007 Oct 26

PMID : 17724034






5 Functional Relationships(s)
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1 Human 4F2hc expressed in several cell types resulted in cell surface and Cys(109) disulfide bridge-linked homodimers with major architectural features of the crystal dimer, as demonstrated by cross-linking experiments. Cysteine solute carrier family 3 member 2 Homo sapiens
2 Human 4F2hc expressed in several cell types resulted in cell surface and Cys(109) disulfide bridge-linked homodimers with major architectural features of the crystal dimer, as demonstrated by cross-linking experiments. Disulfides solute carrier family 3 member 2 Homo sapiens
3 This location of the N terminus and the Cys(109)-intervening disulfide bridge imposes space restrictions sufficient to support a model for electrostatic interaction of the 4F2hc ectodomain with membrane phospholipids. Cysteine solute carrier family 3 member 2 Homo sapiens
4 This location of the N terminus and the Cys(109)-intervening disulfide bridge imposes space restrictions sufficient to support a model for electrostatic interaction of the 4F2hc ectodomain with membrane phospholipids. Disulfides solute carrier family 3 member 2 Homo sapiens
5 This location of the N terminus and the Cys(109)-intervening disulfide bridge imposes space restrictions sufficient to support a model for electrostatic interaction of the 4F2hc ectodomain with membrane phospholipids. Phospholipids solute carrier family 3 member 2 Homo sapiens