Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction

Background: Proteins belonging to the phosphatidylethanolamine-binding protein (PEBP) family are highly conserved throughout nature and have no significant sequence homology with other proteins of known structure or function. A variety of biological roles have previously been described for members o...

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Veröffentlicht in:	Structure (London) 1998-10, Vol.6 (10), p.1245-1254
Hauptverfasser:	Banfield, Mark J, Barker, John J, Perry, Anthony CF, Brady, R Leo
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Androgen-Binding Protein Animals Binding Sites Carrier Proteins - chemistry Carrier Proteins - physiology Cell Membrane - physiology crystal structure Crystallography, X-Ray hippocampal neurostimulatory peptide precursor Humans Models, Molecular Molecular Sequence Data Phosphatidylcholines - metabolism Phosphatidylethanolamine Binding Protein Phospholipid Transfer Proteins Protein Conformation Sequence Alignment Sequence Homology, Amino Acid Signal Transduction - physiology signalling
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