Publications

Displaying 1 - 25 of 105

Effects of Glycans and Hinge on Dynamics in the IgG1 Fc

October 28, 2023

Author(s)

Christina Bergonzo, J. Todd Hoopes, Zvi Kelman, David Travis Gallagher

The crystallizable fragment (Fc) domain of immunoglobulin subclass IgG1 antibodies is engineered for a wide variety of pharmaceutical applications. Two important structural variables in Fc constructs are the hinge region connecting the Fc to the antigen

Design and characterization of a protein fold switching network

January 26, 2023

Author(s)

David Travis Gallagher, Biao Ruan, Yanan He, Yingwei Chen, Eun Jung Choi, Yihong Chen, Dana Motabar, Tsega Solomon, Richard Simmerman, Thomas Kauffman, John Orban, Philip Bryan

Protein sequences encoding three common small folds (3-alpha, beta-grasp, and alpha/beta plait) were connected in a network of mutational pathways that intersect at high-identity sequences, termed nodes. The structures of proteins around nodes were

Reversible switching between two common protein folds in a designed system using only temperature

January 19, 2023

Author(s)

Tsega Solomon, Yanan He, Fahriye Nese Sari, Yihong Chen, David Travis Gallagher, Philip Bryan, John Orban

Naturally occurring metamorphic proteins have the ability to interconvert from one folded state to another through either a limited set of mutations or by way of a change in the local environment. Here, we show that it is possible to switch reversibly

Atomic Model Structure of the NIST Monoclonal Antibody (NISTmAb) Reference Material

July 15, 2021

Author(s)

Christina Bergonzo, David Travis Gallagher

As monoclonal antibodies have become a vital resource in medicine, knowledge of their complex molecular structures has increased in importance. Thousands of antibody components (Fab and Fc fragments) are described in the Protein Data Bank. Whole antibodies

Crystal Structure of a Bivalent Antibody Fab Fragment

November 11, 2020

Author(s)

Salman Shahid, Mingming Gao, David Travis Gallagher, Steven Foung, Zhen-Yong Keck, Thomas Fuerst, Roy Mariuzza

We determined the crystal structure to 1.8 Å resolution of the Fab fragment of an affinity- matured human monoclonal antibody (HC84.26.5D) that recognizes the E2 envelope glycoprotein of hepatitis C virus (HCV). Unlike conventional Fabs, which are

Structure and Dynamics of a Site-Specific Labeled Fc Fragment with Altered Effector Functions

October 21, 2019

Author(s)

David T. Gallagher, Robert G. Brinson, John P. Marino, nazzareno dimasi

Antibody-drug conjugates (ADCs) are a class of biotherapeutic drugs designed as targeted therapies for the treatment of cancer. Among the challenges in generating an effective ADC is the choice of an effective conjugation site on the IgG. One common method

Structure of the Fc Fragment from the NIST Reference Antibody RM8671

September 1, 2018

Author(s)

David Travis Gallagher, Connor V. Galvin, Ioannis Karageorgos

As the link between antigen binding and immune activation, the antibody Fc region has received extensive structural study. In this report, the structure of the Fc fragment of the NIST IgG1 mAb (reference material 8671) is described at 2.1 Å resolution in

Data on crystal organization in the structure of the Fab fragment from the NIST reference antibody, RM 8671

December 1, 2017

Author(s)

David T. Gallagher, Ioannis L. Karageorgos, Jeffrey W. Hudgens, Connor V. Galvin

This article describes the crystal packing of the unliganded antibody fragment from the NIST reference antibody 8671, whose atomic coordinates are available as Protein Data Bank structure 5K8A [1]. Here we give information on the crystallization and

Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

December 1, 2017

Author(s)

Darion Spigolon, David Travis Gallagher, Adrian Velazquez-Campoy, Donatella Bulone, Jatin Narang, Pier San Biagio, Francesco Cappello, Alberto J. Macario, Everly Conway de Macario, Frank Robb

The human chaperonin complex is a 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy

Biophysical Characterization and Structure of the Fab Fragment from the NIST Reference Antibody RM 8671

September 29, 2017

Author(s)

Ioannis Karageorgos, Elyssia S. Gallagher, Connor Galvin, David Travis Gallagher, Jeffrey W. Hudgens

Monoclonal antibody (mAb) pharmaceuticals are the fastest-growing class of therapeutics with a wide range of clinical applications. To assure their safety, these protein drugs must demonstrate highly consistent purity and stability. Key to these objectives

Chorismate Lyase at 0.9 Resolution

February 19, 2017

Author(s)

David Travis Gallagher, A Howard

Chorismate

A Bacteriophage Endolysin that Eliminates Intracellular Streptococci

March 15, 2016

Author(s)

Yang Shen, Marilia Barros, Tarek Vennemann, David Travis Gallagher, Yizhou Yin, Sara B. Linden, Ryan D. Heselpoth, Dennis J. Spencer, David M. Donovan, John Moult, Vincent A. Fischetti, Frank Heinrich, Mathias Loesche, Daniel C. Nelson

PlyC, a bacteriophage-encoded A-B endolysin, lyses Streptococcus pyogenes (Spy) on contact and protects mice from upper respiratory Spy colonization. Here, we demonstrate that PlyC is a novel, potent agent for targeting and controlling intracellular Spy

Current and Emerging Technologies to Characterize the Higher-Order Structure of Monoclonal Antibodies

October 15, 2015

Author(s)

John Marino, Robert G. Brinson, Jane E. Ladner, David Travis Gallagher, Luke Arbogast, Richard Huang, Jeffrey W. Hudgens, Elyssia S. Gallagher

In contrast to small molecule therapeutics whose conformations can be absolutely defined by constitution and stereochemistry, biopharmaceuticals are distinguished by the requirement for folding into higher order structures (secondary, tertiary, and

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