1JT5

Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L73V/V109L)

1JT5 の概要

• エントリーDOI: 10.2210/pdb1jt5/pdb
• 関連するPDBエントリー: 1JQZ
• 分子名称: acidic fibroblast growth factor, SULFATE ION (3 entities in total)
• 機能のキーワード: beta-trefoil, hormone-growth factor complex, hormone/growth factor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P05230
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33757.75

構造登録者

Brych, S.R.,Blaber, S.I.,Logan, T.M.,Blaber, M. (登録日: 2001-08-20, 公開日: 2001-12-19, 最終更新日: 2023-08-16)

主引用文献

Brych, S.R.,Blaber, S.I.,Logan, T.M.,Blaber, M.
Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.
Protein Sci., 10:2587-2599, 2001

PubMed Abstract: Human acidic fibroblast growth factor (FGF-1) is a member of the beta-trefoil hyperfamily and exhibits a characteristic threefold symmetry of the tertiary structure. However, evidence of this symmetry is not readily apparent at the level of the primary sequence. This suggests that while selective pressures may exist to retain (or converge upon) a symmetric tertiary structure, other selective pressures have resulted in divergence of the primary sequence during evolution. Using intra-chain and homologue sequence comparisons for 19 members of this family of proteins, we have designed mutants of FGF-1 that constrain a subset of core-packing residues to threefold symmetry at the level of the primary sequence. The consequences of these mutations regarding structure and stability were evaluated using a combination of X-ray crystallography and differential scanning calorimetry. The mutational effects on structure and stability can be rationalized through the characterization of "microcavities" within the core detected using a 1.0A probe radius. The results show that the symmetric constraint within the primary sequence is compatible with a well-packed core and near wild-type stability. However, despite the general maintenance of overall thermal stability, a noticeable increase in non-two-state denaturation follows the increase in primary sequence symmetry. Therefore, properties of folding, rather than stability, may contribute to the selective pressure for asymmetric primary core sequences within symmetric protein architectures.

PubMed: 11714927
DOI: 10.1110/ps.ps.34701

実験手法

X-RAY DIFFRACTION (1.85 Å)