Crystal Structure of Basic Fibroblast Growth Factor at 1.6.ANGS. Resolution.
-
- Ago Hideo
- Institute for Protein Research, Osaka University
-
- Kitagawa Yasuyuki
- Institute for Protein Research, Osaka University
-
- Fujishima Akira
- Biotechnology Research Laboratories, Research and Development Division, Takeda Chemical Industries, Ltd.
-
- Matsuura Yoshiki
- Institute for Protein Research, Osaka University
-
- Katsube Yukiteru
- Institute for Protein Research, Osaka University
この論文をさがす
説明
We have determined the crystal structures of two types of human basic fibroblast growth factor, the serine analogue and the wild-type, at 1.6 and 2.5 Å resolution, respectively. Two good heavy atom derivatives were found and used for multiple isomorphous replacement phasing. The atomic coordinates were refined using the Hendrickson & Konnert program for stereochemically restrained refinement against structure factors. The crystallographic R factors were reduced to 15.3% for the serine analogue structure and 16.0% for the wild-type structure. The serine analogue and wild-type structures have been found to be almost identical, the root-mean-square deviation between the corresponding Cα atoms being 0.11Å. Their structures are composed of twelve β-strands forming a barrel and three loops. Their molecules have an approximate threefold internal symmetry and are similar in architecture to that of interleukin-1 β. A possible heparin-binding site, which comprises five basic residues, Lys119, Arg120, Lys125, Lys129, and Lys135, has been revealed by calculating the electrostatic potential energy.
収録刊行物
-
- The Journal of Biochemistry
-
The Journal of Biochemistry 110 (3), 360-363, 1991
The Japanese Biochemical Society
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1571980078057156992
-
- NII論文ID
- 130003531488
-
- ISSN
- 0021924X
-
- 本文言語コード
- en
-
- データソース種別
-
- CiNii Articles