Trans-Sialidase-Like Sequences from Trypanosoma congolense Conserve Most of the Critical Active Site Residues Found in Other Trans-Sialidases
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| 024 | 7 | 0 | |a 10.1515/BC.2003.133 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2003.133 | ||
| 245 | 0 | 0 | |a Trans-Sialidase-Like Sequences from Trypanosoma congolense Conserve Most of the Critical Active Site Residues Found in Other Trans-Sialidases |h [Elektronische Daten] |c [E. Tiralongo, I. Martensen, J. Grötzinger, J. Tiralongo, R. Schauer] |
| 520 | 3 | |a Trypanosoma congolense is the agent of Nagana, the trypanosomiasis in African ruminants. Trypanosomes express an enzyme called trans-sialidase, which is believed to play an important role in maintaining pathogenicity of the parasites. Thus far, only two complete trans-sialidase sequences have been characterised, one from the American trypanosome T. cruzi and one from the African trypanosome T. brucei brucei. Although the crystal structure of T. cruzi trans-sialidase has recently been published [Buschiazzo et al., Mol. Cell 10 (2002), pp. 757 768], a number of questions concerning the exact transfer mechanism remain unanswered. The availability of further trans-sialidase sequences will ensure a better understanding of how transfer activity can be achieved and will provide the opportunity to develop highly specific, structure-based trans-sialidase inhibitors. Utilising a PCR-based approach two different trans-sialidase gene copies from T. congolense were identified, which share only 50% identity with each other, but show significant similarity with known viral, bacterial and trypanosomal sialidases and trans-sialidases. In both partial sequences most of the critical active site residues common to other trypanosomal sialidases and trans-sialidases are conserved. This is further illustrated by modelling the active site of the longer of the two partial gene sequences. | |
| 540 | |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 700 | 1 | |a Tiralongo |D E. |4 aut | |
| 700 | 1 | |a Martensen |D I. |4 aut | |
| 700 | 1 | |a Grötzinger |D J. |4 aut | |
| 700 | 1 | |a Tiralongo |D J. |4 aut | |
| 700 | 1 | |a Schauer |D R. |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 384/8(2003-08-20), 1203-1213 |x 1431-6730 |q 384:8<1203 |1 2003 |2 384 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2003.133 |q text/html |z Onlinezugriff via DOI |
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| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2003.133 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tiralongo |D E. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Martensen |D I. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Grötzinger |D J. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tiralongo |D J. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Schauer |D R. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 384/8(2003-08-20), 1203-1213 |x 1431-6730 |q 384:8<1203 |1 2003 |2 384 |o bchm | ||
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