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| - | [[Image:1rg4.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1rg4.png|left|200px]] |
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| | {{STRUCTURE_1rg4| PDB=1rg4 | SCENE= }} | | {{STRUCTURE_1rg4| PDB=1rg4 | SCENE= }} |
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| - | '''SP-B C-terminal peptide in organic solvent (HFIP)'''
| + | ===SP-B C-terminal peptide in organic solvent (HFIP)=== |
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| - | ==Overview==
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| - | Although the membrane-associated surfactant protein B (SP-B) is an essential component of lung surfactant, which is itself essential for life, the molecular basis for its activity is not understood. SP-B's biophysical functions can be partially mimicked by subfragments of the protein, including the C-terminus. We have used NMR to determine the structure of a C-terminal fragment of human SP-B that includes residues 63-78. Structure determination was performed both in the fluorinated alcohol hexafluoro-2-propanol (HFIP) and in sodium dodecyl sulfate (SDS) micelles. In both solvents, residues 68-78 take on an amphipathic helical structure, in agreement with predictions made by comparison to homologous saposin family proteins. In HFIP, the five N-terminal residues of the peptide are largely unstructured, while in SDS micelles, these residues take on a well-defined compact conformation. Differences in helical residue side chain positioning between the two solvents were also found, with better agreement between the structures for the hydrophobic face than the hydrophilic face. A paramagnetic probe was used to investigate the position of the peptide within the SDS micelles and indicated that the peptide is located at the water interface with the hydrophobic face of the helix oriented inward, the hydrophilic face of the helix oriented outward, and the N-terminal residues even farther from the micelle center than those on the hydrophilic face of the alpha-helix. Interactions of basic residues of SP-B with anionic lipid headgroups are known to have an impact on function, and these studies demonstrate structural ramifications of such interactions via the differences observed between the peptide structures determined in HFIP and SDS.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15568810}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15568810 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15568810}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1RG4 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RG4 OCA]. | + | 1RG4 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RG4 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Sp-b]] | | [[Category: Sp-b]] |
| | [[Category: Surfactant]] | | [[Category: Surfactant]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:27:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:39:58 2008'' |
Revision as of 04:40, 29 July 2008
Template:STRUCTURE 1rg4
SP-B C-terminal peptide in organic solvent (HFIP)
Template:ABSTRACT PUBMED 15568810
About this Structure
1RG4 is a Single protein structure. Full experimental information is available from OCA.
Reference
NMR structures of the C-terminal segment of surfactant protein B in detergent micelles and hexafluoro-2-propanol., Booth V, Waring AJ, Walther FJ, Keough KM, Biochemistry. 2004 Dec 7;43(48):15187-94. PMID:15568810
Page seeded by OCA on Tue Jul 29 07:39:58 2008
