1dfw
From Proteopedia
(Difference between revisions)
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| - | + | ==CONFORMATIONAL MAPPING OF THE N-TERMINAL SEGMENT OF SURFACTANT PROTEIN B IN LIPID USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)== | |
| - | + | <StructureSection load='1dfw' size='340' side='right' caption='[[1dfw]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1dfw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DFW FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dfw RCSB], [http://www.ebi.ac.uk/pdbsum/1dfw PDBsum]</span></td></tr> |
| - | [[http://www.uniprot.org/uniprot/PSPB_HUMAN PSPB_HUMAN]] Defects in SFTPB are the cause of pulmonary surfactant metabolism dysfunction type 1 (SMDP1) [MIM:[http://omim.org/entry/265120 265120]]; also called pulmonary alveolar proteinosis due to surfactant protein B deficiency. A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress.<ref>PMID:7491219</ref> | + | </table> |
| - | + | == Disease == | |
| - | ==Function== | + | [[http://www.uniprot.org/uniprot/PSPB_HUMAN PSPB_HUMAN]] Defects in SFTPB are the cause of pulmonary surfactant metabolism dysfunction type 1 (SMDP1) [MIM:[http://omim.org/entry/265120 265120]]; also called pulmonary alveolar proteinosis due to surfactant protein B deficiency. A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress.<ref>PMID:7491219</ref> Genetic variations in SFTPB are a cause of susceptibility to respiratory distress syndrome in premature infants (RDS) [MIM:[http://omim.org/entry/267450 267450]]. RDS is a lung disease affecting usually premature newborn infants. It is characterized by deficient gas exchange, diffuse atelectasis, high-permeability lung edema and fibrin-rich alveolar deposits called 'hyaline membranes'. Note=A variation Ile to Thr at position 131 influences the association between specific alleles of SFTPA1 and respiratory distress syndrome in premature infants.<ref>PMID:11063734</ref> |
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/PSPB_HUMAN PSPB_HUMAN]] Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter. | [[http://www.uniprot.org/uniprot/PSPB_HUMAN PSPB_HUMAN]] Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Synthetic peptides based on the N-terminal domain of human surfactant protein B (SP-B1-25; 25 amino acid residues; NH2-FPIPLPYCWLCRALIKRIQAMIPKG) retain important lung activities of the full-length, 79-residue protein. Here, we used physical techniques to examine the secondary conformation of SP-B1-25 in aqueous, lipid and structure-promoting environments. Circular dichroism and conventional, 12C-Fourier transform infrared (FTIR) spectroscopy each indicated a predominate alpha-helical conformation for SP-B1-25 in phosphate-buffered saline, liposomes of 1-palmitoyl-2-oleoyl phosphatidylglycerol and the structure-promoting solvent hexafluoroisopropanol; FTIR spectra also showed significant beta- and random conformations for peptide in these three environments. In further experiments designed to map secondary structure to specific residues, isotope-enhanced FTIR spectroscopy was performed with 1-palmitoyl-2-oleoyl phosphatidylglycerol liposomes and a suite of SP-B1-25 peptides labeled with 13C-carbonyl groups at either single or multiple sites. Combining these 13C-enhanced FTIR results with energy minimizations and molecular simulations indicated the following model for SP-B1-25 in 1-palmitoyl-2-oleoyl phosphatidylglycerol: beta-sheet (residues 1-6), alpha-helix (residues 8-22) and random (residues 23-25) conformations. Analogous structural motifs are observed in the corresponding homologous N-terminal regions of several proteins that also share the 'saposin-like' (i.e. 5-helix bundle) folding pattern of full-length, human SP-B. In future studies, 13C-enhanced FTIR spectroscopy and energy minimizations may be of general use in defining backbone conformations at amino acid resolution, particularly for peptides or proteins in membrane environments. | ||
| - | + | Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy.,Gordon LM, Lee KY, Lipp MM, Zasadzinski JA, Walther FJ, Sherman MA, Waring AJ J Pept Res. 2000 Apr;55(4):330-47. PMID:10798379<ref>PMID:10798379</ref> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Gordon, L M | + | == References == |
| - | [[Category: Lee, K Y.C | + | <references/> |
| - | [[Category: Lipp, M M | + | __TOC__ |
| - | [[Category: Sherman, M A | + | </StructureSection> |
| - | [[Category: Walther, F J | + | [[Category: Gordon, L M]] |
| - | [[Category: Waring, A J | + | [[Category: Lee, K Y.C]] |
| - | [[Category: Zasadzinski, J A | + | [[Category: Lipp, M M]] |
| + | [[Category: Sherman, M A]] | ||
| + | [[Category: Walther, F J]] | ||
| + | [[Category: Waring, A J]] | ||
| + | [[Category: Zasadzinski, J A]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Lung surfactant protein]] | [[Category: Lung surfactant protein]] | ||
[[Category: Saposin]] | [[Category: Saposin]] | ||
Revision as of 12:25, 18 December 2014
CONFORMATIONAL MAPPING OF THE N-TERMINAL SEGMENT OF SURFACTANT PROTEIN B IN LIPID USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)
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