2C55

Solution Structure of the Human Immunodeficiency Virus Type 1 p6 Protein

2C55 の概要

• エントリーDOI: 10.2210/pdb2c55/pdb
• 分子名称: PROTEIN P6 (1 entity in total)
• 機能のキーワード: p6, hiv-1, p6-gag, aids, core protein, lipoprotein, membrane, metal-binding, myristate, phosphorylation, polyprotein, rna-binding, viral nucleoprotein, zinc, zinc-finger, viral protein
• 由来する生物種: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1)
• 細胞内の位置: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential): P12493
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5812.30

構造登録者

Fossen, T.,Wray, V.,Bruns, K.,Rachmat, J.,Henklein, P.,Tessmer, U.,Maczurek, A.,Klinger, P.,Schubert, U. (登録日: 2005-10-25, 公開日: 2005-11-02, 最終更新日: 2024-05-15)

主引用文献

Fossen, T.,Wray, V.,Bruns, K.,Rachmat, J.,Henklein, P.,Tessmer, U.,Maczurek, A.,Klinger, P.,Schubert, U.
Solution Structure of the Human Immunodeficiency Virus Type 1 P6 Protein.
J.Biol.Chem., 280:42515-, 2005

PubMed Abstract: The human immunodeficiency virus type 1 p6 protein represents a docking site for several cellular and viral binding factors and fulfills major roles in the formation of infectious viruses. To date, however, the structure of this 52-amino acid protein, by far the smallest lentiviral protein known, either in its mature form as free p6 or as the C-terminal part of the Pr55 Gag polyprotein has not been unraveled. We have explored the high resolution structure and folding of p6 by CD and NMR spectroscopy. Under membranous solution conditions, p6 can adopt a helix-flexible helix structure; a short helix-1 (amino acids 14-18) is connected to a pronounced helix-2 (amino acids 33-44) by a flexible hinge region. Thus, p6 can be subdivided into two distinct structural and functional domains; helix-2 perfectly defines the region that binds to the virus budding factor AIP-1/ALIX, indicating that this structure is required for interaction with the endosomal sorting complex required for transport. The PTAP motif at the N terminus, comprising the primary late assembly domain, which is crucial for interaction with another cellular budding factor, Tsg101, does not exhibit secondary structure. However, the adjacent helix-1 may play an indirect role in the specific complex formation between p6 and the binding groove in Tsg101. Moreover, binding studies by NMR demonstrate that helix-2, which also comprises the LXXLF motif required for incorporation of the human immunodeficiency virus type 1 accessory protein Vpr into budding virions, specifically interacts with the Vpr binding region, indicating that under the specific solution conditions used for structure analysis, p6 adopted a functional conformation.

PubMed: 16234236
DOI: 10.1074/JBC.M507375200

実験手法

SOLUTION NMR