Structure and Function in Rhodopsin:  Effects of Disulfide Cross-Links in the Cytoplasmic Face of Rhodopsin on Transducin Activation and Phosphorylation by Rhodopsin Kinase†,‡

Biochemistry ◽  
1999 ◽  
Vol 38 (39) ◽  
pp. 12893-12898 ◽  
Author(s):  
Kewen Cai ◽  
Judith Klein-Seetharaman ◽  
John Hwa ◽  
Wayne L. Hubbell ◽  
H. Gobind Khorana
Keyword(s):  
Structure And Function ◽  
Cytoplasmic Face ◽  
Rhodopsin Kinase ◽  
Cross Links ◽  
And Function

Structure of CD20 in complex with the therapeutic monoclonal antibody rituximab

Science ◽  
2020 ◽  
Vol 367 (6483) ◽  
pp. 1224-1230 ◽  
Author(s):  
Lionel Rougé ◽  
Nancy Chiang ◽  
Micah Steffek ◽  
Christine Kugel ◽  
Tristan I. Croll ◽  
...  
Keyword(s):  
Structural Model ◽  
Structure And Function ◽  
Antigen Binding ◽  
Surface Markers ◽  
Cell Surface Markers ◽  
Therapeutic Monoclonal Antibody ◽  
Cross Links ◽  
Cell Membrane Protein ◽  
And Function ◽  
Cluster Of Differentiation

Cluster of differentiation 20 (CD20) is a B cell membrane protein that is targeted by monoclonal antibodies for the treatment of malignancies and autoimmune disorders but whose structure and function are unknown. Rituximab (RTX) has been in clinical use for two decades, but how it activates complement to kill B cells remains poorly understood. We obtained a structure of CD20 in complex with RTX, revealing CD20 as a compact double-barrel dimer bound by two RTX antigen-binding fragments (Fabs), each of which engages a composite epitope and an extensive homotypic Fab:Fab interface. Our data suggest that RTX cross-links CD20 into circular assemblies and lead to a structural model for complement recruitment. Our results further highlight the potential relevance of homotypic Fab:Fab interactions in targeting oligomeric cell-surface markers.

Tyrosine Cross-Links:  Molecular Basis of Gluten Structure and Function

2001 ◽  
Vol 49 (5) ◽  
pp. 2627-2632 ◽  
Author(s):  
Katherine A. Tilley ◽  
Rachel E. Benjamin ◽  
Katherine E. Bagorogoza ◽  
B. Moses Okot-Kotber ◽  
Om Prakash ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Structure And Function ◽  
Cross Links ◽  
And Function ◽  
Gluten Structure

scholarly journals THE FINE STRUCTURE AND FUNCTION OF THE CONTRACTILE AXOSTYLES OF CERTAIN FLAGELLATES

1965 ◽  
Vol 24 (3) ◽  
pp. 387-400 ◽  
Author(s):  
A. V. Grimstone ◽  
L. R. Cleveland
Keyword(s):  
Plasma Membrane ◽  
Fine Structure ◽  
Structure And Function ◽  
Basal Bodies ◽  
Structural Components ◽  
Cross Links ◽  
Cilia And Flagella ◽  
Fine Structure And Function ◽  
And Function ◽  
Regular Arrays

The axostyles of the flagellates Oxymonas, Saccinobaculus, and Notila are large ribbon-shaped structures which undulate actively in the cytoplasm. The form of their movements is described and illustrated. Axostyles consist of regular arrays of longitudinal fibres, the number of which varies between 100 and 5000 in different species. The fibres are about 240 A in diameter, apparently hollow, regularly cross-banded with a periodicity of about 150 A, and connected by delicate cross-links, also at regular intervals of about 150 A. They resemble very closely the central fibres of cilia and flagella. No other structural components are present, except at the anterior end, where the fibres are attached to one or more basal bodies, and at the posterior tip, where they are anchored to the plasma membrane. The relevance of the findings to an understanding of the mechanism of ciliary and flagellar movements is discussed.

Structure and Function of Escherichia Coli Ribosomal Protein L7/L12: Effect of Cross-Links and Deletions

1993 ◽  
pp. 521-532 ◽  
Author(s):  
Robert R. Traut ◽  
Andrew V. Oleinikov ◽  
Evgeny Makarov ◽  
George Jokhadze ◽  
Bertrand Perroud ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Structure And Function ◽  
Cross Links ◽  
And Function

Structure and function of DHHC protein S-acyltransferases

2017 ◽  
Vol 45 (4) ◽  
pp. 923-928 ◽  
Author(s):  
Colin D. Gottlieb ◽  
Maurine E. Linder
Keyword(s):  
Mouse Models ◽  
Protein Function ◽  
Molecular Mechanisms ◽  
Protein S ◽  
Structure And Function ◽  
Deficient Mouse ◽  
Enzymatic Function ◽  
Cytoplasmic Face ◽  
Dhhc Protein ◽  
And Function

It has been estimated that 10% of the human genome encodes proteins that are fatty acylated at cysteine residues. The vast majority of these proteins are modified by members of the DHHC protein family, which carry out their enzymatic function on the cytoplasmic face of cell membranes. The biomedical importance of DHHC proteins is underscored by their association with human disease; unique and essential roles for DHHC proteins have been uncovered using DHHC-deficient mouse models. Accordingly, there is great interest in elucidating the molecular mechanisms that underlie DHHC protein function. In this review, we present recent insights into the structure and function of DHHC enzymes.

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