scholarly journals The solution structure of the transducin-α-uncoordinated 119 protein complex suggests occlusion of the Gβ1γ1-binding sites

FEBS Journal ◽  
2014 ◽  
Vol 282 (3) ◽  
pp. 550-561 ◽  
Author(s):  
Pallavi Cheguru ◽  
Anurima Majumder ◽  
Ravi Yadav ◽  
Kota N. Gopalakrishna ◽  
Lokesh Gakhar ◽  
...  
Keyword(s):  
Protein Complex ◽  
Binding Sites ◽  
Solution Structure

Rat GTP cyclohydrolase I is a homodecameric protein complex containing high-affinity calcium-binding sites 1 1Edited by W. Baumeister

1998 ◽  
Vol 279 (1) ◽  
pp. 189-199 ◽  
Author(s):  
Michel O Steinmetz ◽  
Christoph Plüss ◽  
Urs Christen ◽  
Bettina Wolpensinger ◽  
Ariel Lustig ◽  
...  
Keyword(s):  
Protein Complex ◽  
Binding Sites ◽  
Calcium Binding ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase ◽  
High Affinity ◽  
Calcium Binding Sites

Solution Structure of Eps15's Third EH Domain Reveals Coincident Phe−Trp and Asn−Pro−Phe Binding Sites†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (15) ◽  
pp. 4309-4319 ◽  
Author(s):  
Jennifer L. Enmon ◽  
Tonny de Beer ◽  
Michael Overduin
Keyword(s):  
Binding Sites ◽  
Solution Structure ◽  
Eh Domain

scholarly journals Binding of Phosphorylated Sp1 Protein to Tandem Sp1 Binding Sites Regulates α2 Integrin Gene Core Promoter Activity

Blood ◽  
1997 ◽  
Vol 90 (2) ◽  
pp. 678-689 ◽  
Author(s):  
Mary M. Zutter ◽  
Ellen E. Ryan ◽  
Audrey D. Painter
Keyword(s):  
Complex Formation ◽  
Protein Complex ◽  
Binding Sites ◽  
Promoter Activity ◽  
Core Promoter ◽  
K562 Cells ◽  
The Core ◽  
Nuclear Extracts ◽  
Integrin Gene ◽  
Α2β1 Integrin

Abstract The α2β1 integrin, a collagen/laminin receptor, is expressed by a variety of cell types, including epithelial cells, mesenchymal cells, and hematopoietic cells. To understand the molecular mechanisms that regulate expression of the α2β1 integrin in cells with megakaryocytic differentiation, we characterized the 5′ flanking region of the α2 integrin gene and identified three distinct regulatory regions, including a core promoter, a silencer, and megakaryocyte enhancers in the distal 5′ flank (Zutter et al, Blood 96:3006, 1995 and Zutter et al, J Biol Chem 269:463, 1994). We now focus on the core promoter of the α2 integrin gene located between bp −30 and −92 that is required for transcriptional activity of the α2 integrin gene. Sequence analysis identified two Sp1 consensus sites and a potential AP2 site. Gel retardation assays showed that nuclear proteins from uninduced K562 cells and K562 cells induced to become megakaryocytic bound specifically to the core promoter region (bp −30 to bp −92) producing two DNA-protein complexes. In addition, nuclear extracts from cells induced along the megakaryocyte lineage produced a selective increase in the slower migrating complex. Site-directed mutagenesis of the 5′, the 3′, or both Sp1 binding sites suggested that both Sp1 binding sites are required for full promoter activity and for DNA-protein complex formation. DNA footprinting also showed specific protection of the 5′ Sp1 site by nuclear extracts from uninduced K562 cells and protection of both the 5′ and the 3′ Sp1 sites by nuclear extracts from induced K562 cells. Sp1 protein-DNA complex formation was dependent on Sp1 phosphorylation. The faster migrating DNA-protein complex was enhanced by dephosphorylation; the slower migrating DNA-protein complex was diminished or lost.

scholarly journals Structural and Functional Characterization of Cargo-Binding Sites on the μ4-Subunit of Adaptor Protein Complex 4

PLoS ONE ◽  
2014 ◽  
Vol 9 (2) ◽  
pp. e88147 ◽  
Author(s):  
Breyan H. Ross ◽  
Yimo Lin ◽  
Esteban A. Corales ◽  
Patricia V. Burgos ◽  
Gonzalo A. Mardones
Keyword(s):  
Protein Complex ◽  
Binding Sites ◽  
Functional Characterization ◽  
Adaptor Protein ◽  
Cargo Binding

Binding of Phosphorylated Sp1 Protein to Tandem Sp1 Binding Sites Regulates α2 Integrin Gene Core Promoter Activity

Blood ◽  
1997 ◽  
Vol 90 (2) ◽  
pp. 678-689 ◽  
Author(s):  
Mary M. Zutter ◽  
Ellen E. Ryan ◽  
Audrey D. Painter
Keyword(s):  
Complex Formation ◽  
Protein Complex ◽  
Binding Sites ◽  
Promoter Activity ◽  
Core Promoter ◽  
K562 Cells ◽  
The Core ◽  
Nuclear Extracts ◽  
Integrin Gene ◽  
Α2β1 Integrin

The α2β1 integrin, a collagen/laminin receptor, is expressed by a variety of cell types, including epithelial cells, mesenchymal cells, and hematopoietic cells. To understand the molecular mechanisms that regulate expression of the α2β1 integrin in cells with megakaryocytic differentiation, we characterized the 5′ flanking region of the α2 integrin gene and identified three distinct regulatory regions, including a core promoter, a silencer, and megakaryocyte enhancers in the distal 5′ flank (Zutter et al, Blood 96:3006, 1995 and Zutter et al, J Biol Chem 269:463, 1994). We now focus on the core promoter of the α2 integrin gene located between bp −30 and −92 that is required for transcriptional activity of the α2 integrin gene. Sequence analysis identified two Sp1 consensus sites and a potential AP2 site. Gel retardation assays showed that nuclear proteins from uninduced K562 cells and K562 cells induced to become megakaryocytic bound specifically to the core promoter region (bp −30 to bp −92) producing two DNA-protein complexes. In addition, nuclear extracts from cells induced along the megakaryocyte lineage produced a selective increase in the slower migrating complex. Site-directed mutagenesis of the 5′, the 3′, or both Sp1 binding sites suggested that both Sp1 binding sites are required for full promoter activity and for DNA-protein complex formation. DNA footprinting also showed specific protection of the 5′ Sp1 site by nuclear extracts from uninduced K562 cells and protection of both the 5′ and the 3′ Sp1 sites by nuclear extracts from induced K562 cells. Sp1 protein-DNA complex formation was dependent on Sp1 phosphorylation. The faster migrating DNA-protein complex was enhanced by dephosphorylation; the slower migrating DNA-protein complex was diminished or lost.

scholarly journals Structure-Based Functional Analysis of a Hormone Belonging to an Ecdysozoan Peptide Superfamily: Revelation of a Common Molecular Architecture and Residues Possibly for Receptor Interaction

2021 ◽  
Vol 22 (20) ◽  
pp. 11142
Author(s):  
Yun-Ru Chen ◽  
Nai-Wan Hsiao ◽  
Yi-Zong Lee ◽  
Shiau-Shan Huang ◽  
Chih-Chun Chang ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Receptor Binding ◽  
Binding Sites ◽  
Disulfide Bonds ◽  
Solution Structure ◽  
Receptor Interaction ◽  
Resonance Spectroscopy ◽  
Molecular Architecture ◽  
Major Factors

A neuropeptide (Sco-CHH-L), belonging to the crustacean hyperglycemic hormone (CHH) superfamily and preferentially expressed in the pericardial organs (POs) of the mud crab Scylla olivacea, was functionally and structurally studied. Its expression levels were significantly higher than the alternative splice form (Sco-CHH) in the POs, and increased significantly after the animals were subjected to a hypo-osmotic stress. Sco-CHH-L, but not Sco-CHH, significantly stimulated in vitro the Na+, K+-ATPase activity in the posterior (6th) gills. Furthermore, the solution structure of Sco-CHH-L was resolved using nuclear magnetic resonance spectroscopy, revealing that it has an N-terminal tail, three α-helices (α2, Gly9−Asn28; α3, His34−Gly38; and α5, Glu62−Arg72), and a π-helix (π4, Cys43−Tyr54), and is structurally constrained by a pattern of disulfide bonds (Cys7–Cys43, Cys23–Cys39, and Cys26–Cys52), which is characteristic of the CHH superfamily-peptides. Sco-CHH-L is topologically most similar to the molt-inhibiting hormone from the Kuruma prawn Marsupenaeus japonicus with a backbone root-mean-square-deviation of 3.12 Å. Ten residues of Sco-CHH-L were chosen for alanine-substitution, and the resulting mutants were functionally tested using the gill Na+, K+-ATPase activity assay, showing that the functionally important residues (I2, F3, E45, D69, I71, and G73) are located at either end of the sequence, which are sterically close to each other and presumably constitute the receptor binding sites. Sco-CHH-L was compared with other members of the superfamily, revealing a folding pattern, which is suggested to be common for the crustacean members of the superfamily, with the properties of the residues constituting the presumed receptor binding sites being the major factors dictating the ligand–receptor binding specificity.

scholarly journals Solution Structure of CCL19 and Identification of Overlapping CCR7 and PSGL-1 Binding Sites

Biochemistry ◽  
2015 ◽  
Vol 54 (27) ◽  
pp. 4163-4166 ◽  
Author(s):  
Christopher T. Veldkamp ◽  
Eva Kiermaier ◽  
Skylar J. Gabel-Eissens ◽  
Miranda L. Gillitzer ◽  
David R. Lippner ◽  
...  
Keyword(s):  
Binding Sites ◽  
Solution Structure
Sign in / Sign up

Export Citation Format

Share Document