This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2jou

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

NMR structure of Mini-B, an N-terminal- C-terminal construct from human Surfactant Protein-B (SP-B), in Hexafluoroisopropanol (HFIP)

Structural highlights

2jou is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2a2h. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Surfactant protein B (SP-B) is essential for normal lung surfactant function, which is in itself essential to life. However, the molecular basis for SP-B's activity is not understood and a high-resolution structure for SP-B has not been determined. Mini-B is a 34-residue peptide with internal disulfide linkages that is composed of the N- and C-terminal helical regions of SP-B. It has been shown to retain similar activity to full-length SP-B in certain in vitro and in vivo studies. We have used solution NMR to determine the structure of Mini-B in the presence of micelles composed of the anionic detergent sodium dodecyl sulfate (SDS). Under these conditions, Mini-B forms two alpha-helices connected by an unstructured loop. Mini-B possesses a strikingly amphipathic surface with a large positively charged patch on one face of the peptide and a large hydrophobic patch on the opposite face. A tryptophan side chain extends outward from the peptide in a position to interact with lipids at the polar/apolar interface. Interhelix interactions are stabilized by both disulfide bonds and by interleaving of hydrophobic side chains from the two helices.

Structure of mini-B, a functional fragment of surfactant protein B, in detergent micelles.,Sarker M, Waring AJ, Walther FJ, Keough KM, Booth V Biochemistry. 2007 Oct 2;46(39):11047-56. Epub 2007 Sep 11. PMID:17845058^[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
↑ Sarker M, Waring AJ, Walther FJ, Keough KM, Booth V. Structure of mini-B, a functional fragment of surfactant protein B, in detergent micelles. Biochemistry. 2007 Oct 2;46(39):11047-56. Epub 2007 Sep 11. PMID:17845058 doi:http://dx.doi.org/10.1021/bi7011756

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/2jou"

@@ Line 1: / Line 1: @@
 ==NMR structure of Mini-B, an N-terminal- C-terminal construct from human Surfactant Protein-B (SP-B), in Hexafluoroisopropanol (HFIP)==
-<StructureSection load='2jou' size='340' side='right'caption='[[2jou]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
+<StructureSection load='2jou' size='340' side='right'caption='[[2jou]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jou]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2a2h 2a2h]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JOU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2jou]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2a2h 2a2h]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JOU FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rg3|1rg3]], [[1rg4|1rg4]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jou OCA], [https://pdbe.org/2jou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jou RCSB], [https://www.ebi.ac.uk/pdbsum/2jou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jou ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/PSPB_HUMAN PSPB_HUMAN]] Defects in SFTPB are the cause of pulmonary surfactant metabolism dysfunction type 1 (SMDP1) [MIM:[https://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:[https://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>
+[https://www.uniprot.org/uniprot/PSPB_HUMAN PSPB_HUMAN] Defects in SFTPB are the cause of pulmonary surfactant metabolism dysfunction type 1 (SMDP1) [MIM:[https://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:[https://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 ==
-[[https://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.
+[https://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 ==
@@ Line 24: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Booth, V]]
+[[Category: Booth V]]
-[[Category: Keough, K M.W]]
+[[Category: Keough KMW]]
-[[Category: Sarker, M]]
+[[Category: Sarker M]]
-[[Category: Walther, F J]]
+[[Category: Walther FJ]]
-[[Category: Waring, A J]]
+[[Category: Waring AJ]]
-[[Category: Lipid associated protein]]
-[[Category: Mini-b]]
-[[Category: Sp-b]]
-[[Category: Surface active protein]]
-[[Category: Surfactant protein b]]

2jou

From Proteopedia

Current revision

NMR structure of Mini-B, an N-terminal- C-terminal construct from human Surfactant Protein-B (SP-B), in Hexafluoroisopropanol (HFIP)

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox