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

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 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 a Repeated Unit of the ABA-1 Nematode Polyprotein Allergen of Ascaris Reveals a Novel Fold and Two Discrete Lipid-Binding Sites

2011 ◽  
Vol 5 (4) ◽  
pp. e1040 ◽  
Author(s):  
Nicola A. G. Meenan ◽  
Graeme Ball ◽  
Krystyna Bromek ◽  
Dušan Uhrín ◽  
Alan Cooper ◽  
...  
Keyword(s):  
Binding Sites ◽  
Solution Structure ◽  
Lipid Binding ◽  
Repeated Unit

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

scholarly journals Recognition and targeting mechanisms by chaperones in flagellum assembly and operation

2016 ◽  
Vol 113 (35) ◽  
pp. 9798-9803 ◽  
Author(s):  
Nandish Khanra ◽  
Paolo Rossi ◽  
Anastassios Economou ◽  
Charalampos G. Kalodimos
Keyword(s):  
Membrane Protein ◽  
Binding Sites ◽  
Solution Structure ◽  
Hydrophobic Surface ◽  
The Other ◽  
Capping Protein ◽  
Substrate Complex ◽  
Substrate Protein ◽  
Flagellar Proteins ◽  
Substrate Proteins

The flagellum is a complex bacterial nanomachine that requires the proper assembly of several different proteins for its function. Dedicated chaperones are central in preventing aggregation or undesired interactions of flagellar proteins, including their targeting to the export gate. FliT is a key flagellar chaperone that binds to several flagellar proteins in the cytoplasm, including its cognate filament-capping protein FliD. We have determined the solution structure of the FliT chaperone in the free state and in complex with FliD and the flagellar ATPase FliI. FliT adopts a four-helix bundle and uses a hydrophobic surface formed by the first three helices to recognize its substrate proteins. We show that the fourth helix constitutes the binding site for FlhA, a membrane protein at the export gate. In the absence of a substrate protein FliT adopts an autoinhibited structure wherein both the binding sites for substrates and FlhA are occluded. Substrate binding to FliT activates the complex for FlhA binding and thus targeting of the chaperone–substrate complex to the export gate. The activation and targeting mechanisms reported for FliT appear to be shared among the other flagellar chaperones.

scholarly journals Structure-based functional study of a peptide of an ecdysozoan superfamily: reveling a common molecular architecture and receptor-interacting residues

2020 ◽  
Author(s):  
Yun-Ru Chen ◽  
Nai-Wan Hsiao ◽  
Shiau-Shan Huang ◽  
Chih-Chun Chang ◽  
Yi-Zong Lee ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Receptor Binding ◽  
Binding Sites ◽  
Disulfide Bonds ◽  
Solution Structure ◽  
Functional Study ◽  
Resonance Spectroscopy ◽  
Molecular Architecture ◽  
Major Factors

ABSTRACTA 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 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, 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; α5, Glu62−Arg72), and a π-helix (π4, Cys43−Tyr53) and is structurally constrained by a pattern of disulfide bonds (Cys7-Cys43, Cys23-Cys39, 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-substituted 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, G73) are located at either end of the sequence, which are sterically close to each other and presumably constitutes the receptor binding sites. Sco-CHH-L was compared with other members of the superfamily revealing a molecular architecture, 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 Structural basis for client recognition and activity of Hsp40 chaperones

Science ◽  
2019 ◽  
Vol 365 (6459) ◽  
pp. 1313-1319 ◽  
Author(s):  
Yajun Jiang ◽  
Paolo Rossi ◽  
Charalampos G. Kalodimos
Keyword(s):  
Binding Sites ◽  
Solution Structure ◽  
Structural Basis ◽  
Resonance Spectroscopy ◽  
Dynamic Features ◽  
Atomic Structures ◽  
Binding Domains ◽  
Wide Range ◽  
Distinct Sequence ◽  
And Function

Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes including protein synthesis, membrane translocation, and folding. We used nuclear magnetic resonance spectroscopy to determine the solution structure and dynamic features of an Hsp40 in complex with an unfolded client protein. Atomic structures of the various binding sites in the client complexed to the binding domains of the Hsp40 reveal the recognition pattern. Hsp40 engages the client in a highly dynamic fashion using a multivalent binding mechanism that alters the folding properties of the client. Different Hsp40 family members have different numbers of client-binding sites with distinct sequence selectivity, providing additional mechanisms for activity regulation and function modification. Hsp70 binding to Hsp40 displaces the unfolded client. The activity of Hsp40 is altered in its complex with Hsp70, further regulating client binding and release.

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