Active Conformation and Mimetic Analog Development for the Pyrokinin—PBAN—Diapause—Pupariation and Myosuppressin Insect Neuropeptide Families

1997 ◽  
pp. 277-291 ◽  
Author(s):  
Ronald J. Nachman ◽  
Victoria A. Roberts ◽  
Angela B. Lange ◽  
Ian Orchard ◽  
G. Mark Holman ◽  
...  
Keyword(s):  
Active Conformation ◽  
Insect Neuropeptide

scholarly journals Active conformation of an insect neuropeptide family.

1991 ◽  
Vol 88 (10) ◽  
pp. 4518-4522 ◽  
Author(s):  
R. J. Nachman ◽  
V. A. Roberts ◽  
H. J. Dyson ◽  
G. M. Holman ◽  
J. A. Tainer
Keyword(s):  
Active Conformation ◽  
Insect Neuropeptide

Modeling the Active Conformation of Human µ Opioid Receptor

2014 ◽  
Vol 11 (9) ◽  
pp. 1053-1061 ◽  
Author(s):  
Agnieszka Kaczor ◽  
Damian Bartuzi ◽  
Dariusz Matosiuk
Keyword(s):  
Opioid Receptor ◽  
Active Conformation

The Role of the N-Terminal Domain in the Regulation of the “Constitutively Active” Conformation of Protein Kinase CK2α: Insight from a Molecular Dynamics Investigation

ChemMedChem ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. 1207-1216 ◽  
Author(s):  
Andrea Cristiani ◽  
Giorgio Costa ◽  
Giorgio Cozza ◽  
Flavio Meggio ◽  
Leonardo Scapozza ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Protein Kinase ◽  
Active Conformation ◽  
Terminal Domain ◽  
Constitutively Active

scholarly journals A Novel, Enzymatically Active Conformation of theEscherichia coliNADH:Ubiquinone Oxidoreductase (Complex I)

2002 ◽  
Vol 277 (20) ◽  
pp. 17970-17977 ◽  
Author(s):  
Bettina Böttcher ◽  
Dierk Scheide ◽  
Micaela Hesterberg ◽  
Luitgard Nagel-Steger ◽  
Thorsten Friedrich
Keyword(s):  
Complex I ◽  
Active Conformation

scholarly journals The C-terminal residue of phage Vp16 PDF, the smallest peptide deformylase, acts as an offset element locking the active conformation

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Renata Grzela ◽  
Julien Nusbaum ◽  
Sonia Fieulaine ◽  
Francesco Lavecchia ◽  
Willy V. Bienvenut ◽  
...  
Keyword(s):  
Peptide Deformylase ◽  
Active Conformation ◽  
Terminal Residue

Insect neuropeptide F (NPF)-related peptides: Isolation from colorado potato beetle (Leptinotarsa decemlineata) brain

1996 ◽  
Vol 26 (4) ◽  
pp. 375-382 ◽  
Author(s):  
Kurt Spittaels ◽  
Peter Verhaert ◽  
Chris Shaw ◽  
Richard N. Johnston ◽  
Bart Devreese ◽  
...  
Keyword(s):  
Colorado Potato Beetle ◽  
Leptinotarsa Decemlineata ◽  
Insect Neuropeptide ◽  
Potato Beetle ◽  
Neuropeptide F

scholarly journals Structure of TFIIK for phosphorylation of CTD of RNA polymerase II

2021 ◽  
Vol 7 (15) ◽  
pp. eabd4420
Author(s):  
Trevor van Eeuwen ◽  
Tao Li ◽  
Hee Jong Kim ◽  
Jose J. Gorbea Colón ◽  
Mitchell I. Parker ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Transcription Initiation ◽  
Activation Loop ◽  
Active Conformation ◽  
General Transcription Factor ◽  
Cryo Electron Microscopy ◽  
Proposed Model ◽  
Carboxyl Terminal ◽  
Catalytic Cleft

During transcription initiation, the general transcription factor TFIIH marks RNA polymerase II by phosphorylating Ser5 of the carboxyl-terminal domain (CTD) of Rpb1, which is followed by extensive modifications coupled to transcription elongation, mRNA processing, and histone dynamics. We have determined a 3.5-Å resolution cryo–electron microscopy (cryo-EM) structure of the TFIIH kinase module (TFIIK in yeast), which is composed of Kin28, Ccl1, and Tfb3, yeast homologs of CDK7, cyclin H, and MAT1, respectively. The carboxyl-terminal region of Tfb3 was lying at the edge of catalytic cleft of Kin28, where a conserved Tfb3 helix served to stabilize the activation loop in its active conformation. By combining the structure of TFIIK with the previous cryo-EM structure of the preinitiation complex, we extend the previously proposed model of the CTD path to the active site of TFIIK.

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