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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Pietrzyk, Agnieszka J. Bujacz, Anna Mak, Pawel Potempa, Barbara Niedziela, Tomasz |
| Description | Country affiliation: Poland Author Affiliation: Pietrzyk AJ ( Institute of Technical Biochemistry, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, Stefanowskiego 4/10, Lodz 90-924, Poland.); Bujacz A ( Institute of Technical Biochemistry, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, Stefanowskiego 4/10, Lodz 90-924, Poland. Electronic address: anna.bujacz@p.lodz.pl.); Mak P ( Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7A, 30-387 Krakow, Poland); Potempa B ( University of Louisville School of Dentistry, Department of Oral Immunology and Infectious Diseases, 501 South Preston Street, Louisville, KY 40202, USA.); Niedziela T ( Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Rudolfa Weigla 12, Wroclaw 53-114, Poland.) |
| Abstract | Lectins belong to a differentiated group of proteins known to possess sugar-binding properties. Due to this fact, they are interesting research targets in medical diagnostics. Helix aspersa agglutinin (HAA) is a lectin that recognizes the epitopes containing -d-N-acetylgalactosamine (GalNAc), which is present at the surface of metastatic cancer cells. Although several reports have already described the use of HAA as a diagnostic tool, this protein was not characterized on the molecular level. Here, we present for the first time the structural information about lectin isolated from mucus of Helix aspersa (garden snail). The amino acid sequence of this agglutinin was determined by Edman degradation and tertiary as well as quaternary structure by X-ray crystallography. The high resolution crystal structure (1.38Å) and MALDI-TOF mass spectrometry analysis provide the detailed information about a large part of the HAA natural glycan chain. The topology of the GalNAc binding cleft and interaction with lectin are very well defined in the structure and fully confirmed by STD HSQC NMR spectroscopy. Together, this provides structural clues regarding HAA specificity and opens possibilities to rational modifications of this important diagnostic tool. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 81 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-11-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Agglutinins Chemistry Galactosamine Snails Amino Acid Sequence Animals Binding Sites Chromatography, High Pressure Liquid Chromatography, Reverse-phase Epitope Mapping Glycosylation Magnetic Resonance Spectroscopy Molecular Sequence Data Protein Isoforms Metabolism Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization Static Electricity X-ray Diffraction Zinc Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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