Sandbox Reserved 654: Difference between revisions

Line 17:

== Structure ==

The bromodomain was originally identified as a sequence of roughly 60 amino acid residues that forms 2 alpha helices. Haynes, S.R. et al (1992) Nucleic Acids Res. 20, 2603. However, it is now known that the bromodomain consist of a highly conserved sequence of approximately 110 amino acids. Owen, D. J. et al. (2000) EMBO J. 19(22), 6141. The structure of the PCAF bromodomain consists of a <scene name='Sandbox_Reserved_654/Four-helix/1'>four-helix</scene> bundle (alphaZ, aA,aB, and aC) with a left-handed twist, and a long intervening loop between helices Z and A (ZA loop). Dhalluin. The ZA loop of the bromodomain has a defined conformation and is packed against the loop between helices aB and aC (BC loop) to form a hydrophobic pocket. This pocket created by the ZA and BC loops is lined by specific residues (Val 752, Ala 757, Tyr 760, Val 763, Tyr 802 and Tyr 809) that support protein-protein interactions. The ZA loop varies in length between different bromodomains, but almost always contains residues corresponding to Phe 748, Pro 751, Pro 758, Tyr 760 and Pro 767. Dhalluin.

The bromodomain was originally identified as a sequence of roughly 60 amino acid residues that forms 2 alpha helices<ref>Haynes, S.R. et al (1992) Nucleic Acids Res. 20, 2603 [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC312404/]</ref>. However, it is now known that the bromodomain consist of a highly conserved sequence of approximately 110 amino acids<ref> Owen, D. J. et al. (2000) EMBO J. 19(22), 6141 [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC305837/]</ref>. The structure of the PCAF bromodomain consists of a <scene name='Sandbox_Reserved_654/Four-helix/1'>four-helix</scene> bundle (alphaZ, aA,aB, and aC) with a left-handed twist, and a long intervening loop between helices Z and A (ZA loop). Dhalluin. The ZA loop of the bromodomain has a defined conformation and is packed against the loop between helices aB and aC (BC loop) to form a hydrophobic pocket. This pocket created by the ZA and BC loops is lined by specific residues (Val 752, Ala 757, Tyr 760, Val 763, Tyr 802 and Tyr 809) that support protein-protein interactions. The ZA loop varies in length between different bromodomains, but almost always contains residues corresponding to Phe 748, Pro 751, Pro 758, Tyr 760 and Pro 767. Dhalluin.

== Function ==

Sandbox Reserved 654: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 17: / Line 17: @@
 == Structure ==
-The bromodomain was originally identified as a sequence of roughly 60 amino acid residues that forms 2 alpha helices. Haynes, S.R. et al (1992) Nucleic Acids Res. 20, 2603. However, it is now known that the bromodomain consist of a highly conserved sequence of approximately 110 amino acids. Owen, D. J. et al. (2000) EMBO J. 19(22), 6141. The structure of the PCAF bromodomain consists of a <scene name='Sandbox_Reserved_654/Four-helix/1'>four-helix</scene> bundle (alphaZ, aA,aB, and aC) with a left-handed twist, and a long intervening loop between helices Z and A (ZA loop). Dhalluin. The ZA loop of the bromodomain has a defined conformation and is packed against the loop between helices aB and aC (BC loop) to form a hydrophobic pocket. This pocket created by the ZA and BC loops is lined by specific residues (Val 752, Ala 757, Tyr 760, Val 763, Tyr 802 and Tyr 809) that support protein-protein interactions. The ZA loop varies in length between different bromodomains, but almost always contains residues corresponding to Phe 748, Pro 751, Pro 758, Tyr 760 and Pro 767. Dhalluin.
+The bromodomain was originally identified as a sequence of roughly 60 amino acid residues that forms 2 alpha helices<ref>Haynes, S.R. et al (1992) Nucleic Acids Res. 20, 2603 [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC312404/]</ref>. However, it is now known that the bromodomain consist of a highly conserved sequence of approximately 110 amino acids<ref> Owen, D. J. et al. (2000) EMBO J. 19(22), 6141 [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC305837/]</ref>. The structure of the PCAF bromodomain consists of a <scene name='Sandbox_Reserved_654/Four-helix/1'>four-helix</scene> bundle (alphaZ, aA,aB, and aC) with a left-handed twist, and a long intervening loop between helices Z and A (ZA loop). Dhalluin. The ZA loop of the bromodomain has a defined conformation and is packed against the loop between helices aB and aC (BC loop) to form a hydrophobic pocket. This pocket created by the ZA and BC loops is lined by specific residues (Val 752, Ala 757, Tyr 760, Val 763, Tyr 802 and Tyr 809) that support protein-protein interactions. The ZA loop varies in length between different bromodomains, but almost always contains residues corresponding to Phe 748, Pro 751, Pro 758, Tyr 760 and Pro 767. Dhalluin.
 == Function ==