1FYN
PHOSPHOTRANSFERASE
1FYN の概要
| エントリーDOI | 10.2210/pdb1fyn/pdb |
| 分子名称 | PHOSPHOTRANSFERASE FYN, 3BP-2 (3 entities in total) |
| 機能のキーワード | proto-oncogene, transferase, tyrosine-protein kinase, phosphorylation, atp-binding, myristylation, sh3 domain, complex (phosphotransferase-peptide) |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Cell membrane: P06241 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 7984.69 |
| 構造登録者 | |
| 主引用文献 | Musacchio, A.,Saraste, M.,Wilmanns, M. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat.Struct.Biol., 1:546-551, 1994 Cited by PubMed Abstract: Src-homology 3 (SH3) domains bind to proline-rich motifs in target proteins. We have determined high-resolution crystal structures of the complexes between the SH3 domains of Abl and Fyn tyrosine kinases, and two ten-residue proline-rich peptides derived from the SH3-binding proteins 3BP-1 and 3BP-2. The X-ray data show that the basic mode of binding of both proline-rich peptides is the same. Peptides are bound over their entire length and interact with three major sites on the SH3 molecules by both hydrogen-bonding and van der Waals contacts. Residues 4-10 of the peptide adopt the conformation of a left-handed polyproline helix type II. Binding of the proline at position 2 requires a kink at the non-proline position 3. PubMed: 7664083DOI: 10.1038/nsb0894-546 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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