1M16

Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V).

1M16 の概要

• エントリーDOI: 10.2210/pdb1m16/pdb
• 関連するPDBエントリー: 1JQZ
• 分子名称: acidic fibroblast growth factor, SULFATE ION, FORMIC ACID, ... (4 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: 33717.68

構造登録者

Brych, S.R.,Kim, J.,Spielmann, G.L.,Logan, T.M.,Blaber, M. (登録日: 2002-06-17, 公開日: 2003-08-05, 最終更新日: 2024-02-14)

主引用文献

Brych, S.R.,Kim, J.,Logan, T.M.,Blaber, M.
Accommodation of a highly symmetric core within a symmetric protein superfold
Protein Sci., 12:2704-2718, 2003

PubMed Abstract: An alternative core packing group, involving a set of five positions, has been introduced into human acidic FGF-1. This alternative group was designed so as to constrain the primary structure within the core region to the same threefold symmetry present in the tertiary structure of the protein fold (the beta-trefoil superfold). The alternative core is essentially indistinguishable from the WT core with regard to structure, stability, and folding kinetics. The results show that the beta-trefoil superfold is compatible with a threefold symmetric constraint on the core region, as might be the case if the superfold arose as a result of gene duplication/fusion events. Furthermore, this new core arrangement can form the basis of a structural "building block" that can greatly simplify the de novo design of beta-trefoil proteins by using symmetric structural complementarity. Remaining asymmetry within the core appears to be related to asymmetry in the tertiary structure associated with receptor and heparin binding functionality of the growth factor.

PubMed: 14627732
DOI: 10.1110/ps.03374903

実験手法

X-RAY DIFFRACTION (1.7 Å)