Sandbox Reserved 973: Difference between revisions

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=== PAS-A domain ===

PAS-A domains don't have the same conformation in the two subunits. In <scene name='60/604492/Bmal1/1'>BMAL1</scene>, we can observe 3 loops involving about 60 residues whereas in CLOCK there are only 25 residues in a single loop <ref>Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex

PAS-A domains don't have the same conformation in the two subunits. In <scene name='60/604492/Bmal1/1'>BMAL1</scene>, we can observe 3 loops involving about 60 residues whereas in CLOCK there are only 25 residues in a single loop <ref>Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex by

Nian Huang, Yogarany Chelliah, Yongli Shan, Clinton A. Taylor, Seung-Hee Yoo, Carrie Partch, Carla B. Green, Hong Zhang, and Joseph S. Takahashi</ref>. Nevertheless, these two PAS-A domains adopt a typical PAS fold. The core of these domains contains a five-stranded antiparallel β-sheet (AβBβGβHβIβ) as well as numerous α helices (Cα, DαEαFα). They also contain an N-terminal A'α helix that does not belong to the canonical PAS fold. Those helices pack in between the β-sheet faces and are involved in the dimerization interactions.

The two PAS-A domains are mostly linked thanks to hydrophobic bonds. Indeed, Phe104, Leu105, and Leu113 on the A′α helix of CLOCK are interacting with the residues Leu159 on strand Aβ, Thr285 and Tyr287 on Hβ, Val315 and Ile317 on strand Iβ, of the <scene name='60/604492/Bmal1/1'>BMAL1</scene> subunit. The same kind of bonds are occuring between the A'α helix of BMAL1 and the β-sheet of CLOCK. Thus, the two PAS-A domains form a parallel dimer.

Sandbox Reserved 973: Difference between revisions

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 === PAS-A domain ===
-PAS-A domains don't have the same conformation in the two subunits. In <scene name='60/604492/Bmal1/1'>BMAL1</scene>, we can observe 3 loops involving about 60 residues whereas in CLOCK there are only 25 residues in a single loop <ref>Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex
+PAS-A domains don't have the same conformation in the two subunits. In <scene name='60/604492/Bmal1/1'>BMAL1</scene>, we can observe 3 loops involving about 60 residues whereas in CLOCK there are only 25 residues in a single loop <ref>Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex by
 Nian Huang, Yogarany Chelliah, Yongli Shan, Clinton A. Taylor, Seung-Hee Yoo, Carrie Partch, Carla B. Green, Hong Zhang, and Joseph S. Takahashi</ref>. Nevertheless, these two PAS-A domains adopt a typical PAS fold. The core of these domains contains a five-stranded antiparallel β-sheet (AβBβGβHβIβ) as well as numerous α helices (Cα, DαEαFα). They also contain an N-terminal A'α helix that does not belong to the canonical PAS fold. Those helices pack in between the β-sheet faces and are involved in the dimerization interactions.
 The two PAS-A domains are mostly linked thanks to hydrophobic bonds. Indeed, Phe104, Leu105, and Leu113 on the A′α helix of CLOCK are interacting with the residues Leu159 on strand Aβ, Thr285 and Tyr287 on Hβ, Val315 and Ile317 on strand Iβ, of the <scene name='60/604492/Bmal1/1'>BMAL1</scene> subunit. The same kind of bonds are occuring between the A'α helix of BMAL1 and the β-sheet of CLOCK. Thus, the two PAS-A domains form a parallel dimer.