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Literature DB >> 9334742

Saposin fold revealed by the NMR structure of NK-lysin.

E Liepinsh, M Andersson, J M Ruysschaert, G Otting.

Abstract

NK-lysin is the first representative of a family of sequence related proteins--saposins, surfactant-associated protein B, pore forming amoeba proteins, and domains of acid sphingomyelinase, acyloxyacylhydrolase and plant aspartic proteinases--for which a structure has been determined.

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Year: 1997 PMID： 9334742 DOI： 10.1038/nsb1097-793

Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368

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Cited

53 in total

1. Circularly permuted proteins in the protein structure database.

Authors: J Jung; B Lee
Journal: Protein Sci Date: 2001-09 Impact factor: 6.725

2. Direct simulation of protein-mediated vesicle fusion: lung surfactant protein B.

Authors: Svetlana Baoukina; D Peter Tieleman
Journal: Biophys J Date: 2010-10-06 Impact factor: 4.033

3. Effect of pulmonary surfactant protein SP-B on the micro- and nanostructure of phospholipid films.

Authors: Antonio Cruz; Luis Vázquez; Marisela Vélez; Jesús Pérez-Gil
Journal: Biophys J Date: 2004-01 Impact factor: 4.033

4. Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: a comparative functional analysis.

Authors: Heike Bruhn; Beate Riekens; Otto Berninghausen; Matthias Leippe
Journal: Biochem J Date: 2003-11-01 Impact factor: 3.857

Saposin fold revealed by the NMR structure of NK-lysin.

1. Circularly permuted proteins in the protein structure database.

2. Direct simulation of protein-mediated vesicle fusion: lung surfactant protein B.

3. Effect of pulmonary surfactant protein SP-B on the micro- and nanostructure of phospholipid films.

4. Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: a comparative functional analysis.

5. DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a.

6. Cholesterol in negatively charged lipid bilayers modulates the effect of the antimicrobial protein granulysin.

7. NMR experiments for the sign determination of homonuclear scalar and residual dipolar couplings.

8. Surfactant protein B propeptide contains a saposin-like protein domain with antimicrobial activity at low pH.

9. NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B.

Review 10. Saposins and their interaction with lipids.