Structure and Stability of an Acidic Fibroblast Growth Factor from Notophthalmus viridescens
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چکیده
منابع مشابه
Heterogeneity in the expression of fibroblast growth factor receptors during limb regeneration in newts (Notophthalmus viridescens).
Two closely related fibroblast growth factor receptors, FGFR1 and FGFR2, have been cloned from a newt (Notophthalmus viridescens) limb blastema cDNA library. Sequence analysis revealed that we have isolated both the bek and KGFR variants of FGFR2. These two variants differ only in the second half of the last of their three Ig-like domains. The expression patterns of FGFR1 and FGFR2 during limb ...
متن کاملX-ray crystal structure of human acidic fibroblast growth factor.
Fibroblast growth factors (FGFs) are mitogenic and chemotactic agents for a wide variety of cell types and play a primary role in the regulation of angiogenesis. Angiogenesis is involved in a variety of critical physiological events including organogenesis, wound healing, ischemic collateral circulation, and solid tumor growth. High-resolution structural information is key to understanding the ...
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Isoelectric focusing has allowed us to fractionate pituitary extracts into basic (pI 8-9) and acidic (pI 4-5) fibroblast growth factor. The acidic fibroblast growth factor (a) is stable upon refocusing, (b) migrates as an acidic protein in urea-containing gel electrophoresis; (c) is not cell-specific, being active with fibroblasts, adrenal, and glial cells, and (d) is a heterogeneous protein fr...
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The terrestrial red eft stage is so different from the body form of the aquatic adult of the eastern newt that the two were considered separate species for nearly 60 years. Some populations lack the eft stage whereas in other populations the adults are aquatic only during the breeding season. In populations in which the adults are permanently aquatic or migrate to breeding ponds in fall, an aut...
متن کاملMutagenesis of the crystal contact of acidic fibroblast growth factor
An attempt has been made to improve a crystal contact of human acidic fibroblast growth factor (haFGF; 140 amino acids) to control the crystal growth, because haFGF crystallizes only as a thin-plate form, yielding crystals suitable for X-ray but not neutron diffraction. X-ray crystal analysis of haFGF showed that the Glu81 side chain, located at a crystal contact between haFGF molecules, is in ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m207814200