View source for 1bd9

[[Image:1bd9.gif|left|200px]]<br />
<applet load="1bd9" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1bd9, resolution 2.05&Aring;" />
'''HUMAN PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN'''<br />

==Overview==
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 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., RESULTS: The crystal structures of two forms of hPEBP have been, determined: one in the native state (at 2.05 A resolution) and one in, complex with cacodylate (at 1.75 A resolution). The crystal structures, reveal that hPEBP adopts a novel protein topology, dominated by the, presence of a large central beta sheet, and is expected to represent the, archaetypal fold for this family of proteins. Two potential functional, sites have been identified from the structure: a putative ligand-binding, site and a coupled cleavage site. hPEBP forms a dimer in the crystal with, a distinctive dipole moment that may orient the oligomer for membrane, binding. CONCLUSIONS: The crystal structure of hPEBP suggests that the, ligand-binding site could accommodate the phosphate head groups of, membrane lipids, therefore allowing the protein to adhere to the inner, leaf of bilipid membranes where it would be ideally positioned to relay, signals from the membrane to the cytoplasm. The structure also suggests, that ligand binding may lead to coordinated release of the N-terminal, region of the protein to form the hippocampal neurostimulatory peptide, which is known to be active in the development of the hippocampus. These, studies are consistent with a primary biological role for hPEBP as a, transducer of signals from the interior membrane surface.

==Disease==
Known diseases associated with this structure: Cleidocranial dysplasia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600211 600211]], Dental anomalies, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600211 600211]]

==About this Structure==
1BD9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BD9 OCA]. 

==Reference==
Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction., Banfield MJ, Barker JJ, Perry AC, Brady RL, Structure. 1998 Oct 15;6(10):1245-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9782050 9782050]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Banfield, M.J.]]
[[Category: Barker, J.J.]]
[[Category: Brady, R.L.]]
[[Category: Perry, A.C.F.]]
[[Category: lipid-binding]]
[[Category: signalling]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:08:51 2007''