Structure of hisactophilin is similar to interleukin-1-beta and fibroblast growth factor
Article Abstract:
The structure of the protein hisactophilin clarifies its exact physiological role, which is to attach to actin and create filament bundles that allow the actin-containing cytoskeleton to react to chemoattractants. The structure, determined through nuclear magnetic resonance spectroscopy, is characterized by 31 histidine residues, 118 amino acids and a molecular mass of 13.5K. The morphology of hisactophilin resembles that of interleukin-1-beta and fibroblast growth factor although its amino-acid sequence is different.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
User Contributions:
Comment about this article or add new information about this topic:
Structure in solution of the major cold-shock protein from Bacillus subtilis
Article Abstract:
A three-dimensional structure of CspB model shows that the cold-shock domain (CSD) is present in various eukaryotic transcriptional factors and causes the specific binding of a cis-element identified as the Y-box(1-3) to DNA. The form of the CspB is ascertained by the nuclear magnetic resonance spectroscopy. Turns and loops link the 67-residue protein with anti-parallel five stranded beta-barrel, while single-strands bind DNA to CspB in gel retardation experiments.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
User Contributions:
Comment about this article or add new information about this topic:
Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
Article Abstract:
Research on the structure of ectodomain, and fibroblast growth factor, is examined in detail.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport
- Abstracts: Suppression of experimental glomerulonephritis by antiserum against transforming growth factor beta1. Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease
- Abstracts: The structure of malaria pigment beta-haematin. The mean free path for electron conduction in metallic fullerenes
- Abstracts: Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex
- Abstracts: Structure of guanine-nucleotide-exchange factor human Mss4 and identification of its Rab-interacting surface. Crystal structure of a streptococcal protein G domain bound to an Fab fragment