A5013242108- S100 Proteins and Annexins
- Enzyme Structure and Function
- Neonatal Respiratory Health Research
- Lipid Membrane Structure and Behavior
- Glycosylation and Glycoproteins Research
- Influenza Virus Research Studies
- Protein Structure and Dynamics
- Bacillus and Francisella bacterial research
- Hemoglobin structure and function
- Inhalation and Respiratory Drug Delivery
- Enzyme Production and Characterization
- Respiratory viral infections research
- Protease and Inhibitor Mechanisms
- Computational Drug Discovery Methods
- Blood Coagulation and Thrombosis Mechanisms
- Carbohydrate Chemistry and Synthesis
- Immune Response and Inflammation
- Poxvirus research and outbreaks
- Mass Spectrometry Techniques and Applications
- Bacteriophages and microbial interactions
- Peptidase Inhibition and Analysis
- Amino Acid Enzymes and Metabolism
- Bacterial Genetics and Biotechnology
- Metabolism and Genetic Disorders
- Cellular transport and secretion
Boston University
2009-2018
ETH Zurich
2009
Rutgers, The State University of New Jersey
1998-2008
Boston College
2001-2008
BOKU University
2007
University of Cincinnati Medical Center
2003
University of Cincinnati
1998-2001
University of Groningen
2001
Harvard University
1989-1990
Yale University
1989
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analog intermediate on reaction pathwayRobert C. Davenport, Paul A. Bash, Barbara Seaton, Martin Karplus, Gregory Petsko, and Dagmar RingeCite this: Biochemistry 1991, 30, 24, 5821–5826Publication Date (Print):June 18, 1991Publication History Published online1 May 2002Published inissue 18 June...
Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, ion channel activity. The crystal structure rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously structures, all four domains bound calcium this structure. Calcium binding the third domain induced large relocation calcium-binding loop regions, exposing single tryptophan residue...
The interaction between calmodulin and its target protein is a key step in many calcium-regulated cellular functions. Melittin binds tightly to the presence of calcium competitive inhibitor function. Using melittin as model for peptide calmodulin, we have found large Ca2+-dependent conformational change solution induced by binding. Mg2+ does not substitute Ca2+ producing conformation change. Small-angle x-ray scattering has shown that exists dumbbell solution, similar observed crystalline...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTCalcium-induced increase in the radius of gyration and maximum dimension calmodulin measured by small-angle x-ray scatteringB. A. Seaton, J. F. Head, D. M. Engelman, RichardsCite this: Biochemistry 1985, 24, 6740–6743Publication Date (Print):November 19, 1985Publication History Published online1 May 2002Published inissue 19 November 1985https://pubs.acs.org/doi/10.1021/bi00345a002https://doi.org/10.1021/bi00345a002research-articleACS...
Surfactant protein A (SP-A), one of four proteins associated with pulmonary surfactant, binds high affinity to alveolar phospholipid membranes, positioning the at first line defense against inhaled pathogens. SP-A exhibits both calcium-dependent carbohydrate binding, a characteristic collectin family, and specific interactions lipid membrane components. The crystal structure trimeric recognition domain neck was solved 2.1-Å resolution multiwavelength anomalous dispersion phasing from...
Lactadherin is a phosphatidyl-L-serine (Ptd-L-Ser)-binding protein that decorates membranes of milk fat globules. The major Ptd-l-Ser binding function lactadherin has been localized to its C2 domain, which shares homology with the domains blood coagulation factor VIII and V. Correlating this homology, purified competes efficiently factors V for Ptd-L-Ser sites, functioning as potent anticoagulant. We have determined crystal structure domain (Lact-C2) at 1.7A resolution. bovine Lact-C2...
The quaternary structure of annexin V, a calcium‐dependent phospholipid binding protein, was investigated by chemical cross‐linking. Calcium found to induce the formation trimers, hexamers, and higher aggregates only when anionic phospholipids were present. Oligomerization occurred under same conditions as annexin—vesicle binding. A model is proposed in cell stimulation leads calcium‐induced organization arrays V lining inner membrane surface, thus altering properties such permeability fluidity.
Site-directed mutagenesis, electron microscopy, and X-ray crystallography were used to probe the structural basis of annexin IV-induced membrane aggregation inhibition this property by protein kinase C phosphorylation. mutants that either mimic (Thr6Asp, T6D) or prevent (Thr6Ala, T6A) phosphorylation threonine 6 produced for these studies compared with wild-type IV. In vitro assays showed unmodified IV T6A mutant, but not PKC-phosphorylated T6D promote vesicle aggregation. Electron...
Surfactant protein D (SP-D) plays important roles in antiviral host defense. Although SP-D shows a preference for glucose/maltose, the also recognizes d-mannose and variety of mannose-rich microbial ligands. This latter prompted an examination mechanisms mannose recognition, particularly as they relate to high-mannose viral glycans. Trimeric neck plus carbohydrate recognition domains from human (hNCRD) preferred α1−2-linked dimannose (DM) over branched trimannose (TM) core, α1−3 or α1−6 DM,...
Fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) from the cortex of pig kidney and its complexes with either fructose 2,6-bisphosphate (Fru-2,6-P2) or adenosine monophosphate (AMP) have been crystallized in space group P3(2)21. The three-dimensional structure native enzyme has solved at 3.0-A resolution by multiple isomorphous replacement method refined 2.8-A to a crystallographic R factor 0.194. A total 316 335 residues, omitting disordered regions...
Lipopolysaccharides (LPS) of Gram-negative bacteria are important mediators bacterial virulence that can elicit potent endotoxic effects. Surfactant protein D (SP-D) shows specific interactions with LPS, both in vitro and vivo. These involve binding the carbohydrate recognition domain (CRD) to LPS oligosaccharides (OS); however, little is known about mechanisms recognition. Recombinant neck+CRDs (NCRDs) provide an opportunity directly correlate a crystallographic analysis mechanism. In these...
The recognition of influenza A virus (IAV) by surfactant protein D (SP-D) is mediated interactions between the SP-D carbohydrate domains (CRD) and glycans displayed on envelope glycoproteins. Although native human shows potent antiviral aggregating activity, trimeric recombinant neck+CRDs (NCRDs) show little or no capacity to influence IAV infection. mutant NCRD, D325A/R343V, showed marked hemagglutination inhibition viral neutralization, with aggregation aggregation-dependent uptake...
Surfactant protein A (SP-A) is a collagenous C-type lectin (collectin) that critical for pulmonary defense against inhaled microorganisms. Bifunctional avidity of SP-A pathogen-associated molecular patterns (PAMPs) such as lipid and dipalmitoylphosphatidylcholine (DPPC), the major component surfactant membranes lining air-liquid interface lung, ensures poised first-line interactions with pathogens. To improve our understanding motifs are required microbes structures, we explored role...
The energetics and kinetics of the interaction heparin with Ca +2 phospholipid binding protein annexin V, was examined minimum oligosaccharide sequence within that binds V identified. Affinity chromatography studies confirmed dependence this interaction. Analysis data obtained from surface plasmon resonance afforded a K d ∼21 nM for end‐chain immobilized ∼49 heparan sulfate. Isothermal titration calorimetry showed corresponds to an octasaccharide sequence. ∼1 μM stoichiometry 1:1.