Structural studies on calmodulin - novel modes of binding of calmodulin to target enzyme sequences from phosphofructokinase
4РП — Обучение и мобилност на изследователи
- Период
- 1998-10-05 → 2000-04-04
- Финансиране от ЕС
- —
- Участници
- 1
- Схема
- RGI
Линиите свързват координатора с партньорите.
Накратко на български
Протеинът калмодулин и начинът, по който той се свързва с ензима фосфофруктокиназа, се анализират чрез ядреномагнитен резонанс. Това помага да се разбере как се променя структурата на протеина, когато той спира работата на този конкретен ензим.
Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.
Цел на проекта
Research objectives and content Calmodulin is a calcium binding protein ( 148 residues) which can respond to changes in calcium concentration and cause activation of a number of important enzymes. High resolution structures have been reported for calmodulin complexed with target peptides from muscle myosin light chain kinases and calmodulin kinase II. These show the 'canonical' structure of a largely helical peptide embedded between the two domains of calmodulin. In the case of the phosphofructokinase, the regulation is unusual in that Ca2+ -calmodulin causes inhibition of the enzyme. Peptides from its target sequence for calmodulin binding have been synthesised and Circular Dichroism studies of their complexes with calmodulin suggest that these peptides have a different mode of interaction: the characterisation of this conformation could provide the first high resolution structural evidence of a target conformation other than the canonical form. The object of this project is to determine the conformation of the bound peptides and the structure of their binding sites using multidimensional Nuclear Magnetic Resonance methods (including isotopic editing techniques) on calmodulin-peptide complexes. Labelled (15N/ 13C) calmodulin has already been prepared and a detailed set of multidimensional NMR experiments will be carried out to determine the constraints required to calculate the structures of the complexes. Training content (objective, benefit and expected Impact) Learning to use apply modern multidimensional Nuclear Magnetic Resonance techniques for examining protein-ligand complexes and for determining their structures. Methods for examining multiligand binding will be learnt. Circular Dichroism and other spectroscopic techniques will also be used. Links with industry / industrial relevance (22) There is no direct links with industry but the project could provide overall improvements in methods of studying and understanding protein-ligand complexes in solution which could be of general interest to the pharmaceutical industry.
Оригинален текст от CORDIS (на английски).
Участници
- MEDICAL RESEARCH COUNCIL · LONDONКоординаторОбединеното кралство
Връзки
Данни: CORDIS, © Европейски съюз