Related ArticlesWhat function for human lithostathine?: structural investigations by three-dimensional structure modeling and high-resolution NMR spectroscopy.
Protein Eng. 1996 Nov;9(11):949-57
Authors: Patard L, Stoven V, Gharib B, Bontems F, Lallemand JY, De Reggi M
Human lithostathine is a 144-residue protein, expressed in various organs and pathologies. Several biological functions have been proposed for this protein. Among others, inhibition of nucleation and growth of CaCO3 crystals in the pancreas and bacterial aggregation has retained attention, because lithostathine presents high sequence similarities with calcium-dependent (or C-type) lectins. To study its structure-function relationship and compare it with that of C-type lectins, we have built a model for lithostathine. This model is derived from the only two C-type lectins of known structures: rat mannose binding protein and human E-selectin. An original strategy, inspired by that proposed by Havel and Snow, was designed for model building. We have undertaken NMR studies on the natural protein. Although complete structure determination has not yet been achieved, the NMR studies did confirm the main characteristics of the model. From analysis of the proposed model, we concluded that lithostathine is not expected to present sugar- or calcium-binding properties. Therefore, the mechanisms of bacterial aggregation and inhibition of CaCO3 nucleation and growth have not yet been elucidated.
[NMR paper] Structural investigations of a human calcitonin-derived carrier peptide in a membrane
Structural investigations of a human calcitonin-derived carrier peptide in a membrane environment by solid-state NMR.
Related Articles Structural investigations of a human calcitonin-derived carrier peptide in a membrane environment by solid-state NMR.
Biochemistry. 2004 Oct 5;43(39):12459-68
Authors: Wagner K, Beck-Sickinger AG, Huster D
Previous studies have shown that human calcitonin (hCT) and its C-terminal fragment hCT(9-32) translocate in nasal epithelium. Moreover, hCT(9-32) was used as a carrier to internalize efficiently the green...
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[NMR paper] NMR solution structure of the inserted domain of human leukocyte function associated
NMR solution structure of the inserted domain of human leukocyte function associated antigen-1.
Related Articles NMR solution structure of the inserted domain of human leukocyte function associated antigen-1.
J Mol Biol. 2000 Feb 4;295(5):1251-64
Authors: Legge GB, Kriwacki RW, Chung J, Hommel U, Ramage P, Case DA, Dyson HJ, Wright PE
The interaction between the leukocyte function-associated antigen-1 (LFA-1) and the intercellular adhesion molecule is thought to be mediated primarily via the inserted domain (I-domain) in the alpha-subunit. The...
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[NMR paper] NMR investigations of the role of the sugar moiety in glycosylated recombinant human
NMR investigations of the role of the sugar moiety in glycosylated recombinant human granulocyte-colony-stimulating factor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR investigations of the role of the sugar moiety in glycosylated recombinant human granulocyte-colony-stimulating factor.
Eur J Biochem. 1997 Jul 1;247(1):386-95
Authors: Gervais V, Zerial A, Oschkinat H
Human granulocyte-colony-stimulating factor (G-CSF) is a...
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[NMR paper] NMR investigations of the role of the sugar moiety in glycosylated recombinant human
NMR investigations of the role of the sugar moiety in glycosylated recombinant human granulocyte-colony-stimulating factor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR investigations of the role of the sugar moiety in glycosylated recombinant human granulocyte-colony-stimulating factor.
Eur J Biochem. 1997 Jul 1;247(1):386-95
Authors: Gervais V, Zerial A, Oschkinat H
Human granulocyte-colony-stimulating factor (G-CSF) is a...
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[NMR paper] NMR investigations of the structural properties of the nodulation protein, NodF, from
NMR investigations of the structural properties of the nodulation protein, NodF, from Rhizobium leguminosarum and its homology with Escherichia coli acyl carrier protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR investigations of the structural properties of the nodulation protein, NodF, from Rhizobium leguminosarum and its homology with Escherichia coli acyl carrier protein.
FEBS Lett. 1996 Jun 10;388(1):66-72
Authors: Ghose R, Geiger O, Prestegard JH
...
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[NMR paper] Relationship between electrostatics and redox function in human thioredoxin: characte
Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.
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Biochemistry. 1992 Apr 7;31(13):3442-52
Authors: Forman-Kay JD, Clore GM, Gronenborn AM
The electrostatic behavior of potentially titrating groups in reduced human thioredoxin was investigated...
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[NMR paper] Structure-function relationships in human epidermal growth factor studied by site-dir
Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR.
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Biochemistry. 1991 Sep 10;30(36):8891-8
Authors: Hommel U, Dudgeon TJ, Fallon A, Edwards RM, Campbell ID
In order to elucidate the mechanism of interaction between human epidermal growth factor (EGF) and its receptor, selected variants of EGF, differing by single amino acid substitutions, have been...
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[NMR paper] Structure-function relationships in human epidermal growth factor studied by site-dir
Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR.
Related Articles Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR.
Biochemistry. 1991 Sep 10;30(36):8891-8
Authors: Hommel U, Dudgeon TJ, Fallon A, Edwards RM, Campbell ID
In order to elucidate the mechanism of interaction between human epidermal growth factor (EGF) and its receptor, selected variants of EGF, differing by single amino acid substitutions, have been...