1rg3

From Proteopedia

(Difference between revisions)

Revision as of 11:26, 18 December 2014

SP-B C-terminal peptide in SDS micelles

Structural highlights

1rg3 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1rg4
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[PSPB_HUMAN] Defects in SFTPB are the cause of pulmonary surfactant metabolism dysfunction type 1 (SMDP1) [MIM: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.^[1] Genetic variations in SFTPB are a cause of susceptibility to respiratory distress syndrome in premature infants (RDS) [MIM: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.^[2]

Function

[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.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ballard PL, Nogee LM, Beers MF, Ballard RA, Planer BC, Polk L, deMello DE, Moxley MA, Longmore WJ. Partial deficiency of surfactant protein B in an infant with chronic lung disease. Pediatrics. 1995 Dec;96(6):1046-52. PMID:7491219
↑ Haataja R, Ramet M, Marttila R, Hallman M. Surfactant proteins A and B as interactive genetic determinants of neonatal respiratory distress syndrome. Hum Mol Genet. 2000 Nov 1;9(18):2751-60. PMID:11063734
↑ Booth V, Waring AJ, Walther FJ, Keough KM. NMR structures of the C-terminal segment of surfactant protein B in detergent micelles and hexafluoro-2-propanol. Biochemistry. 2004 Dec 7;43(48):15187-94. PMID:15568810 doi:10.1021/bi0481895

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rg3"

@@ Line 1: / Line 1: @@
-{{STRUCTURE_1rg3|  PDB=1rg3  |  SCENE=  }}
+==SP-B C-terminal peptide in SDS micelles==
-===SP-B C-terminal peptide in SDS micelles===
+<StructureSection load='1rg3' size='340' side='right' caption='[[1rg3]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
-{{ABSTRACT_PUBMED_15568810}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1rg3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RG3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RG3 FirstGlance]. <br>
-==Disease==
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rg4|1rg4]]</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>  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>
+<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=1rg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rg3 RCSB], [http://www.ebi.ac.uk/pdbsum/1rg3 PDBsum]</span></td></tr>
+</table>
-==Function==
+== 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 ==
+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.
-==About this Structure==
+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<ref>PMID:15568810</ref>
-[[1rg3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RG3 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:015568810</ref><references group="xtra"/><references/>
+</div>
-[[Category: Booth, V.]]
+== References ==
-[[Category: Keough, K M.]]
+<references/>
-[[Category: Walther, F J.]]
+__TOC__
-[[Category: Waring, A J.]]
+</StructureSection>
+[[Category: Booth, V]]
+[[Category: Keough, K M]]
+[[Category: Walther, F J]]
+[[Category: Waring, A J]]
 [[Category: Lung]]
 [[Category: Sp-b]]
 [[Category: Surface active protein]]
 [[Category: Surfactant]]

1rg3

From Proteopedia

Revision as of 11:26, 18 December 2014

SP-B C-terminal peptide in SDS micelles

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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