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| - | [[Image:1a44.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1a44.png|left|200px]] |
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| | {{STRUCTURE_1a44| PDB=1a44 | SCENE= }} | | {{STRUCTURE_1a44| PDB=1a44 | SCENE= }} |
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| - | '''PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FROM CALF BRAIN'''
| + | ===PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FROM CALF BRAIN=== |
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| - | ==Overview==
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9782057}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9782057 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9782057}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Zelwer, C.]] | | [[Category: Zelwer, C.]] |
| | [[Category: Lipid-binding]] | | [[Category: Lipid-binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:47:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:00:25 2008'' |
Revision as of 13:00, 30 June 2008
Template:STRUCTURE 1a44
PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FROM CALF BRAIN
Template:ABSTRACT PUBMED 9782057
About this Structure
1A44 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins., Serre L, Vallee B, Bureaud N, Schoentgen F, Zelwer C, Structure. 1998 Oct 15;6(10):1255-65. PMID:9782057
Page seeded by OCA on Mon Jun 30 16:00:25 2008
