1ssz
From Proteopedia
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| - | + | ==Conformational mapping of mini-b: an n-terminal/c-terminal construct of surfactant protein b using 13c-enhanced fourier transform infrared (FTIR) spectroscopy== | |
| - | + | <StructureSection load='1ssz' size='340' side='right' caption='[[1ssz]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[1ssz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SSZ FirstGlance]. <br> | ||
| + | </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=1ssz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ssz RCSB], [http://www.ebi.ac.uk/pdbsum/1ssz PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Surfactant protein B (SP-B) is essential for normal lung surfactant function. Theoretical models predict that the disulfide cross-linked, N- and C-terminal domains of SP-B fold as charged amphipathic helices, and suggest that these adjacent helices participate in critical surfactant activities. This hypothesis is tested using a disulfide-linked construct (Mini-B) based on the primary sequences of the N- and C-terminal domains. Consistent with theoretical predictions of the full-length protein, both isotope-enhanced Fourier transform infrared (FTIR) spectroscopy and molecular modeling confirm the presence of charged amphipathic alpha-helices in Mini-B. Similar to that observed with native SP-B, Mini-B in model surfactant lipid mixtures exhibits marked in vitro activity, with spread films showing near-zero minimum surface tensions during cycling using captive bubble surfactometry. In vivo, Mini-B shows oxygenation and dynamic compliance that compare favorably with that of full-length SP-B. Mini-B variants (i.e. reduced disulfides or cationic residues replaced by uncharged residues) or Mini-B fragments (i.e. unlinked N- and C-terminal domains) produced greatly attenuated in vivo and in vitro surfactant properties. Hence, the combination of structure and charge for the amphipathic alpha-helical N- and C-terminal domains are key to SP-B function. | ||
| - | + | The role of charged amphipathic helices in the structure and function of surfactant protein B.,Waring AJ, Walther FJ, Gordon LM, Hernandez-Juviel JM, Hong T, Sherman MA, Alonso C, Alig T, Braun A, Bacon D, Zasadzinski JA J Pept Res. 2005 Dec;66(6):364-74. PMID:16316452<ref>PMID:16316452</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | <references | + | *[[Alpha-lytic protease|Alpha-lytic protease]] |
| - | [[Category: Alig, T | + | == References == |
| - | [[Category: Alonso, C | + | <references/> |
| - | [[Category: Bacon, D | + | __TOC__ |
| - | [[Category: Braun, A | + | </StructureSection> |
| - | [[Category: Gordon, L M | + | [[Category: Alig, T]] |
| - | [[Category: Hernandez-Juviel, J M | + | [[Category: Alonso, C]] |
| - | [[Category: Hong, T | + | [[Category: Bacon, D]] |
| - | [[Category: Sherman, M A | + | [[Category: Braun, A]] |
| - | [[Category: Walther, F J | + | [[Category: Gordon, L M]] |
| - | [[Category: Waring, A J | + | [[Category: Hernandez-Juviel, J M]] |
| - | [[Category: Zasadzinski, J A | + | [[Category: Hong, T]] |
| + | [[Category: Sherman, M A]] | ||
| + | [[Category: Walther, F J]] | ||
| + | [[Category: Waring, A J]] | ||
| + | [[Category: Zasadzinski, J A]] | ||
[[Category: Lung surfactant protein]] | [[Category: Lung surfactant protein]] | ||
[[Category: Saposin]] | [[Category: Saposin]] | ||
[[Category: Surface active protein]] | [[Category: Surface active protein]] | ||
Revision as of 11:56, 18 December 2014
Conformational mapping of mini-b: an n-terminal/c-terminal construct of surfactant protein b using 13c-enhanced fourier transform infrared (FTIR) spectroscopy
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