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NMR identification of hydrophobic cavities with ow water occupancies in protein structures using small gas molecules

Gottfried Otting
Edvards Liepinsh
Urban Frey
Research01 May 1997
Nature Structural Biology

Volume: 4, P: 396-404
Organic solvents identify specific ligand binding sites on protein surfaces

Edvards Liepinsh
Gottfried Otting
Research01 Mar 1997
Nature Biotechnology

Volume: 15, P: 264-268
Common ancestor of serine proteases and flavin-binding domains

Edvards Liepinsh
Masaya Kitamura
Gottfried Otting
Comments & Opinion01 Feb 1998
Nature Structural Biology

Volume: 5, P: 102-103
Saposin fold revealed by the NMR structure of NK-lysin

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.

Edvards Liepinsh
Mats Andersson
Gottfried Otting
Correspondence01 Oct 1997
Nature Structural Biology

Volume: 4, P: 793-795
Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)

The flavin mononucleotide (FMN)-binding protein from Desulfovibrio vulgaris (Miyazaki F) is structurally related to a so far hypothetical single-domain precursor of chymotrypsin, with the FMN-binding site coinciding with part of the active site of the protease.

Edvards Liepinsh
Masaya Kitamura
Gottfried Otting
Correspondence01 Dec 1997
Nature Structural Biology

Volume: 4, P: 975-979

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NMR identification of hydrophobic cavities with ow water occupancies in protein structures using small gas molecules

Organic solvents identify specific ligand binding sites on protein surfaces

Common ancestor of serine proteases and flavin-binding domains

Saposin fold revealed by the NMR structure of NK-lysin

Pathway of chymotrypsin evolution suggested by the structure of the FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F)

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