JACS 2016

A joint structural refinement against NMR data and X-ray diffraction patterns offers unique opportunities to detect differences in the conformation of biomolecules between the solution and the crystal states. Read More

ChemComm

An integrated approach which combines in-cell NMR spectroscopy with optical and X-ray fluorescence microscopy was developed to describe the intracellular maturation state of human Cu,Zn-SOD1.  Read More

NCB N terminal

Structural and biophysical evidences define the early steps of iron-sulfur protein maturation in the cytosol, demonstrating that  glutaredoxin-3 passes [2Fe-2S] clusters to anamorsin during a protein-protein interaction mediated by their N-terminal domains.  Read More 

nature chemistry

Dynamic nuclear polarization (DNP) in liquid solutions can enhance 13C NMR signals at magnetic fields of 3 T and room temperature up to three orders of magnitude. Read More  Highlighted in Angewandte Chemie

CERM research on covers

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cover J Phys Chem lr  
High relaxivity Gd(III)-DNA gold nanostars: investigation of shape effects on proton relaxation, ACS nano, 9, 3385–3396, 2015 Exploring regions of conformational space occupied by two-domain proteins, J.Phys.Chem.B, 118, 10576-10587, 2014  
NCB N terminal

N-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin

Banci L, Ciofi-Baffoni S, Gajda K, Muzzioli R, Peruzzini R, Winkelmann J.

Nat Chem Biol. 2015 Aug 24. doi: 10.1038/nchembio.1892. [Epub ahead of print]

Abstract

In eukaryotes, cytosolic monothiol glutaredoxins are proteins implicated in intracellular iron trafficking and sensing via their bound [2Fe-2S] clusters. We define a new role of human cytosolic monothiol glutaredoxin-3 (GRX3) in transferring its [2Fe-2S] clusters to human anamorsin, a physical and functional protein partner of GRX3 in the cytosol, whose [2Fe-2S] cluster–bound form is involved in the biogenesis of cytosolic and nuclear Fe-S proteins. Specific protein recognition between the N-terminal domains of the two proteins is the mandatory requisite to promote the [2Fe-2S] cluster transfer from GRX3 to anamorsin.

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PNAS-CCS

 

Human SOD1 maturation through interaction with human CCS

Banci, L. Bertini, I., Cantini, F., Kozyreva, T., Massagni, C., Palumaa, P., Rubino, J.T., Zovo,K.

Proc Natl Acad Sci U S A. 2012; 109(34):13555-60.

Abstract

Copper chaperone for SOD1, CCS, is the physiological partner for the complex mechanism of SOD1 maturation. We report an in vitro model for human CCS-dependent SOD1 maturation based on the study of the interactions of human SOD1 (hSOD1) with full length wild type human CCS (hCCS), as well as with hCCS mutants and various truncated constructs comprising one or two of the protein’s three domains. The synergy between ESI-MS and NMR is fully exploited. This is the first in vitro study of this process at the molecular level. Domain 1 of hCCS is necessary to load hSOD1 with Cu(I), requiring the heterodimeric complex formation with hSOD1 fostered by the interaction with domain 2. Domain 3 is responsible for the catalytic formation of the hSOD1 Cys 57-Cys 146 disulfide bond, which involves both hCCS Cys 244 and Cys 246 via disulfide transfer.

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Featured in Nature Chemical Biology: Research Highlights

 

Selected_2_august2011

 

Structure-based design of a meningococcal antigen inducing broad protective immunity

Scarselli, M., Arico, B., Brunelli, B., Savino, S., Di Marcello, F., Palumbo, E., Veggi, D., Ciucchi, L., Cartocci, E., Comanducci, M., Giuliani, M. M., Cantini, F., Dragonetti, S., Colaprico, A., Doro, F., Giannetti, P., Pallaoro, M., Brogioni, B., Tontini, M., Hilleringmann, M., Nardi Dei, V., Banci, L.

Sci.Trans.Medicine, 3, 91ra62, 2011

Abstract

The sequence variability of protective antigens is a major challenge to the development of vaccines. For Neisseria meningitidis, the bacterial pathogen that causes meningitis, the amino acid sequence of the protective antigen factor H binding protein (fHBP) has more than 300 variations. These sequence differences can be classified into three distinct groups of antigenic variants that do not induce cross-protective immunity. Our goal was to generate a single antigen that would induce immunity against all known sequence variants of N. meningitidis. To achieve this, we rationally designed, expressed, and purified 54 different mutants of fHBP and tested them in mice for the induction of protective immunity. We identified and determined the crystal structure of a lead chimeric antigen that was able to induce high levels of cross-protective antibodies in mice against all variant strains tested. The new fHBP antigen had a conserved backbone that carried an engineered surface containing specificities for all three variant groups. We demonstrate that the structure-based design of multiple immunodominant antigenic surfaces on a single protein scaffold is possible and represents an effective way to create broadly protective vaccines.

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The article has been evaluated by Carlos Morel new 13 Sep 2011 with Rating 10 - Exceptional

Press review

http://www.nature.com/nature/journal/v475/n7356/full/475269a.html

http://www.nature.com/nrd/journal/v10/n9/full/nrd3539.html

http://stm.sciencemag.org/content/3/91/91ps29.full

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http://tokillcancer.com/view/Researchers-Closer-to-Developing-Universal-Meningitis-B-Vaccine_15590.html 

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