1TEN

STRUCTURE OF A FIBRONECTIN TYPE III DOMAIN FROM TENASCIN PHASED BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN

1TEN の概要

• エントリーDOI: 10.2210/pdb1ten/pdb
• 分子名称: TENASCIN (2 entities in total)
• 機能のキーワード: cell adhesion protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P24821
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10061.06

構造登録者

Leahy, D.J.,Hendrickson, W.A.,Aukhil, I.,Erickson, H.P. (登録日: 1992-08-28, 公開日: 1993-10-31, 最終更新日: 2024-02-14)

主引用文献

Leahy, D.J.,Hendrickson, W.A.,Aukhil, I.,Erickson, H.P.
Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein.
Science, 258:987-991, 1992

PubMed Abstract: Fibronectin type III domains are found in many different proteins including cell surface receptors and cell adhesion molecules. The crystal structure of one such domain from the extracellular matrix protein tenascin was determined. The structure was solved by multiwavelength anomalous diffraction (MAD) phasing of the selenomethionyl protein and has been refined to 1.8 angstrom resolution. The folding topology of this domain is identical to that of the extracellular domains of the human growth hormone receptor, the second domain of CD4, and PapD. Although distinct, this topology is similar to that of immunoglobulin constant domains. An Arg-Gly-Asp (RGD) sequence that can function for cell adhesion is found in a tight turn on an exposed loop.

PubMed: 1279805

実験手法

X-RAY DIFFRACTION (1.8 Å)