View source for 2jou


==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]]' scene=''>
== Structural highlights ==
<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='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> 
== 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.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:17845058</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jou" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Booth V]]
[[Category: Keough KMW]]
[[Category: Sarker M]]
[[Category: Walther FJ]]
[[Category: Waring AJ]]