1BEH

HUMAN PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN IN COMPLEX WITH CACODYLATE

Summary for 1BEH

• Entry DOI: 10.2210/pdb1beh/pdb
• Descriptor: PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN, CACODYLATE ION (3 entities in total)
• Functional Keywords: lipid-binding, signalling, lipid binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 42447.55

Authors

Banfield, M.J.,Barker, J.J.,Perry, A.,Brady, R.L. (deposition date: 1998-05-14, release date: 1998-09-16, Last modification date: 2024-05-22)

Primary citation

Banfield, M.J.,Barker, J.J.,Perry, A.C.,Brady, R.L.
Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction.
Structure, 6:1245-1254, 1998

PubMed Abstract: 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 of this family, including lipid binding, roles as odorant effector molecules or opioids, interaction with the cell-signalling machinery, regulation of flowering plant stem architecture, and a function as a precursor protein of a bioactive brain neuropeptide. To date, no experimentally derived structural information has been available for this protein family. In this study we have used X-ray crystallography to determine the three-dimensional structure of human PEBP (hPEBP), in an attempt to clarify the biological role of this unique protein family.

PubMed: 9782050
DOI: 10.1016/S0969-2126(98)00125-7

Experimental method

X-RAY DIFFRACTION (1.75 Å)