1CID

CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS

1CID の概要

• エントリーDOI: 10.2210/pdb1cid/pdb
• 分子名称: T CELL SURFACE GLYCOPROTEIN CD4, SULFATE ION (3 entities in total)
• 機能のキーワード: t-cell surface glycoprotein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P05540
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19802.44

構造登録者

Brady, R.L.,Dodson, E.J.,Lange, G. (登録日: 1993-01-28, 公開日: 1993-07-15, 最終更新日: 2024-11-20)

主引用文献

Brady, R.L.,Dodson, E.J.,Dodson, G.G.,Lange, G.,Davis, S.J.,Williams, A.F.,Barclay, A.N.
Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains.
Science, 260:979-983, 1993

PubMed Abstract: The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with major histocompatibility complex class II antigens and is also a receptor for the human immunodeficiency virus. the extracellular portion of CD4 is predicted to fold into four immunoglobulin-like domains. The crystal structure of the third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and shows that both domains have immunoglobulin folds. Domain 3, however, lacks the disulfide between the beta sheets; this results in an expansion of the domain. There is a difference of 30 degrees in the orientation between domains 3 and 4 when compared with domains 1 and 2. The two CD4 fragment structures provide a basis from which models of the overall receptor can be proposed. These models suggest an extended structure comprising two rigid portions joined by a short and possibly flexible linker region.

PubMed: 8493535

実験手法

X-RAY DIFFRACTION (2.8 Å)