3CQA
Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ala and Lys101Ala
3CQA の概要
| エントリーDOI | 10.2210/pdb3cqa/pdb |
| 分子名称 | Heparin-binding growth factor 1, SULFATE ION, FORMIC ACID, ... (4 entities in total) |
| 機能のキーワード | crystal packing, acetylation, angiogenesis, developmental protein, differentiation, growth factor, heparin-binding, mitogen, polymorphism, hormone |
| 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 | 32872.80 |
| 構造登録者 | Meher, A.K.,Honjo, E.,Kuroki, R.,Lee, J.,Somasundaram, T.,Blaber, M. (登録日: 2008-04-02, 公開日: 2009-04-07, 最終更新日: 2023-08-30) |
| 主引用文献 | Meher, A.K.,Blaber, S.I.,Lee, J.,Honjo, E.,Kuroki, R.,Blaber, M. Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1. Acta Crystallogr.,Sect.F, 65:1136-1140, 2009 Cited by PubMed Abstract: Large-volume protein crystals are a prerequisite for neutron diffraction studies and their production represents a bottleneck in obtaining neutron structures. Many protein crystals that permit the collection of high-resolution X-ray diffraction data are inappropriate for neutron diffraction owing to a plate-type morphology that limits the crystal volume. Human fibroblast growth factor 1 crystallizes in a plate morphology that yields atomic resolution X-ray diffraction data but has insufficient volume for neutron diffraction. The thin physical dimension has been identified as corresponding to the b cell edge and the X-ray structure identified a solvent-mediated crystal contact adjacent to position Glu81 that was hypothesized to limit efficient crystal growth in this dimension. In this report, a series of mutations at this crystal contact designed to both reduce side-chain entropy and replace the solvent-mediated interface with direct side-chain contacts are reported. The results suggest that improved crystal growth is achieved upon the introduction of direct crystal contacts, while little improvement is observed with side-chain entropy-reducing mutations alone. PubMed: 19923735DOI: 10.1107/S1744309109036987 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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