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PDBsum entry 1b7a
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Lipid binding protein
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PDB id
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1b7a
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the phosphatidylethanolamine-Binding protein from bovine brain: a novel structural class of phospholipid-Binding proteins.
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Authors
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L.Serre,
B.Vallée,
N.Bureaud,
F.Schoentgen,
C.Zelwer.
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Ref.
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Structure, 1998,
6,
1255-1265.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: Phosphatidylethanolamine-binding protein (PEBP) is a basic protein
found in numerous tissues from a wide range of species. The screening of gene
and protein data banks defines a family of PEBP-related proteins that are
present in a variety of organisms, including Drosophila and inferior eukaryotes.
PEBP binds to phosphatidylethanolamine and nucleotides in vitro, but its
biological function in vivo is not yet known. The expression of PEBP and related
proteins seems to be correlated with development and cell morphogenesis,
however. To obtain new insights into the PEBP family and its potential
functions, we initiated a crystallographic study of bovine brain PEPB. RESULTS:
The X-ray crystal structure of bovine brain PEBP has been solved using multiple
isomorphous replacement methods, and refined to 1.84 A resolution. The structure
displays a beta fold and exhibits one nonprolyl cis peptide bond. Analysis of
cavities within the structure and sequence alignments were used to identify a
putative ligand-binding site. This binding site is defined by residues of the
C-terminal helix and the residues His85, Asp69, Gly109 and Tyr119. This site
also corresponds to the binding site of phosphorylethanolamine, the polar head
group of phosphatidylethanolamine. CONCLUSIONS: This study shows that PEBP is
not related to the G-protein family nor to known lipid-binding proteins, and
therefore defines a novel structural family of phospholipid-binding proteins.
The PEBP structure contains no internal hydrophobic pocket, as described for
lipocalins or small phospholipid-transfer proteins. Nevertheless, in PEBP, a
small cavity close to the protein surface has a high affinity for anions, such
as phosphate and acetate, and also phosphorylethanolamine. We suggest that this
cavity corresponds to the binding site of the polar head group of
phosphatidylethanolamine.
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Figure 3.
Figure 3. The electrostatic surface potential of PEBP. The
bound phosphorylethanolamine is shown in the cavity in
ball-and-stick representation. Regions of negative potential are
shown in red; regions of positive potential are in blue. The
strip of basic residues is labeled in yellow. CR1 and CR2
represent strand-connecting regions 1 and 2, respectively. (The
figure was created using the program GRASP [25].)
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The above figure is
reprinted
by permission from Cell Press:
Structure
(1998,
6,
1255-1265)
copyright 1998.
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