scholarly journals Investigation of Catalytic Loop Structure, Dynamics, and Function Relationship of Yersinia Protein Tyrosine Phosphatase by Temperature-Jump Relaxation Spectroscopy and X-ray Structural Determination

2012 ◽  
Vol 116 (21) ◽  
pp. 6166-6176 ◽  
Author(s):  
Shan Ke ◽  
Meng-Chiao Ho ◽  
Nickolay Zhadin ◽  
Hua Deng ◽  
Robert Callender
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Temperature Jump ◽  
Tyrosine Phosphatase ◽  
Loop Structure ◽  
X Ray ◽  
Catalytic Loop ◽  
Dynamics And Function ◽  
Function Relationship ◽  
And Function ◽  
Relationship Of

scholarly journals Heavy Atom Detergent/Lipid Combined X-ray Crystallography for Elucidating the Structure-Function Relationships of Membrane Proteins

Membranes ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 823
Author(s):  
Shinya Hanashima ◽  
Takanori Nakane ◽  
Eiichi Mizohata
Keyword(s):  
Membrane Proteins ◽  
Structure Function ◽  
New Technologies ◽  
Heavy Atom ◽  
Protein Structures ◽  
X Ray ◽  
X Ray Crystallography ◽  
Function Relationship ◽  
And Function ◽  
Relationship Of

Membrane proteins reside in the lipid bilayer of biomembranes and the structure and function of these proteins are closely related to their interactions with lipid molecules. Structural analyses of interactions between membrane proteins and lipids or detergents that constitute biological or artificial model membranes are important for understanding the functions and physicochemical properties of membrane proteins and biomembranes. Determination of membrane protein structures is much more difficult when compared with that of soluble proteins, but the development of various new technologies has accelerated the elucidation of the structure-function relationship of membrane proteins. This review summarizes the development of heavy atom derivative detergents and lipids that can be used for structural analysis of membrane proteins and their interactions with detergents/lipids, including their application with X-ray free-electron laser crystallography.

scholarly journals Protein Tyrosine Phosphatase SHP-2 (PTPN11) in Hematopoiesis and Leukemogenesis

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Xia Liu ◽  
Cheng-Kui Qu
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Molecular Mechanisms ◽  
Somatic Mutations ◽  
Tyrosine Phosphatase ◽  
Hematologic Malignancies ◽  
Cytokine Signaling ◽  
Interacting Proteins ◽  
Protein Tyrosine ◽  
And Function ◽  
Shed Light

SHP-2 (PTPN11), a ubiquitously expressed protein tyrosine phosphatase, is critical for hematopoietic cell development and function owing to its essential role in growth factor/cytokine signaling. More importantly, germline and somatic mutations in this phosphatase are associated with Noonan syndrome, Leopard syndrome, and childhood hematologic malignancies. The molecular mechanisms by which SHP-2 mutations induce these diseases are not fully understood, as the biochemical bases of SHP-2 functions still remain elusive. Further understanding SHP-2 signaling activities and identification of its interacting proteins/substrates will shed light on the pathogenesis of PTPN11-associated hematologic malignancies, which, in turn, may lead to novel therapeutics for these diseases.

Structure and Function Relationship of Murine Insulin-like Peptide 5 (INSL5): Free C-Terminus Is Essential for RXFP4 Receptor Binding and Activation

Biochemistry ◽  
2011 ◽  
Vol 50 (39) ◽  
pp. 8352-8361 ◽  
Author(s):  
Alessia Belgi ◽  
Mohammed A. Hossain ◽  
Fazel Shabanpoor ◽  
Linda Chan ◽  
Suode Zhang ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Structure And Function ◽  
C Terminus ◽  
Function Relationship ◽  
Structure And Function Relationship ◽  
And Function ◽  
Relationship Of

Nitrate in the active site of protein tyrosine phosphatase 1B is a putative mimetic of the transition state

2014 ◽  
Vol 70 (2) ◽  
pp. 565-571 ◽  
Author(s):  
Peter W. Kenny ◽  
Janet Newman ◽  
Thomas S. Peat
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Active Site ◽  
Tyrosine Phosphatase ◽  
Nitrate Anion ◽  
Protein Tyrosine Phosphatase 1B ◽  
Tyrosine Residue ◽  
X Ray ◽  
Protein Tyrosine ◽  
Catalytic Cysteine ◽  
Close Contacts

The X-ray crystal structure of the complex of protein tyrosine phosphatase 1B with nitrate anion has been determined and modelled quantum-mechanically. Two protomers were present in the structure, one with the mechanistically important WPD loop closed and the other with this loop open. Nitrate was observed bound to each protomer, making close contacts with the S atom of the catalytic cysteine and a tyrosine residue from a crystallographically related protomer.

scholarly journals X-ray Characterization and Structure-Based Optimization of Striatal-Enriched Protein Tyrosine Phosphatase Inhibitors

2017 ◽  
Vol 60 (22) ◽  
pp. 9299-9319 ◽  
Author(s):  
Michael R. Witten ◽  
Lisa Wissler ◽  
Melanie Snow ◽  
Stefan Geschwindner ◽  
Jon A. Read ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Phosphatase Inhibitors ◽  
X Ray ◽  
Protein Tyrosine

scholarly journals The protein tyrosine phosphatase Pez regulates TGFβ, epithelial–mesenchymal transition, and organ development

2007 ◽  
Vol 178 (7) ◽  
pp. 1223-1235 ◽  
Author(s):  
Leila Wyatt ◽  
Carol Wadham ◽  
Lesley A. Crocker ◽  
Michael Lardelli ◽  
Yeesim Khew-Goodall
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Crucial Role ◽  
Cancer Metastasis ◽  
Epithelial Mesenchymal Transition ◽  
Mdck Cells ◽  
Tyrosine Phosphatase ◽  
Pharyngeal Arches ◽  
Mesenchymal Transition ◽  
Protein Tyrosine ◽  
And Function

Epithelial–mesenchymal transition (EMT), crucial during embryogenesis for new tissue and organ formation, is also considered to be a prerequisite to cancer metastasis. We report here that the protein tyrosine phosphatase Pez is expressed transiently in discrete locations in developing brain, heart, pharyngeal arches, and somites in zebrafish embryos. We also find that Pez knock-down results in defects in these organs, indicating a crucial role in organogenesis. Overexpression of Pez in epithelial MDCK cells causes EMT, with a drastic change in cell morphology and function that is accompanied by changes in gene expression typical of EMT. Transfection of Pez induced TGFβ signaling, critical in developmental EMT with a likely role also in oncogenic EMT. In zebrafish, TGFβ3 is co- expressed with Pez in a number of tissues and its expression was lost from these tissues when Pez expression was knocked down. Together, our data suggest Pez plays a crucial role in organogenesis by inducing TGFβ and EMT.

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