Ramón Hurtado‐Guerrero

Fundacion Agencia Aragonesa para la Investigacion y el Desarrollo

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Francisco Corzana

Universidad de La Rioja

Ismael Compañón

Universidad de La Rioja

Erandi Lira‐Navarrete

University of Copenhagen

Daan M. F. van Aalten

University of Dundee

Jesús M. Peregrina

Universidad de La Rioja

Pedro Merino

Universidad de Zaragoza

Ana García‐García

Universidad de Zaragoza

J. Castro-López

Universidad de Zaragoza

Carme Rovira

Universitat de Barcelona

Henrik Clausen

University of Copenhagen

Cooperative Institutions

Universidad de Zaragoza

129

Consejo Superior de Investigaciones Científicas

University College London

University of York

Newcastle University

Instituto de Investigación Sanitaria Aragón

Centre National de la Recherche Scientifique

University of Copenhagen

Stanford University

University of British Columbia

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The closed conformation of the LDL receptor is destabilized by the low Ca⁺⁺ concentration but favored by the high Mg⁺⁺ concentration in the endosome

FEBS Letters (2015)

Juan Martínez‐Oliván Xabier Arias‐Moreno Ramón Hurtado‐Guerrero José Alberto Carrodeguas Laura Miguel-Romero

The LDL receptor (LDLR) internalizes LDL and VLDL particles. In the endosomes, it adopts a closed conformation important for recycling, by interaction of two modules of the ligand binding domain (LR4–5) and a β‐propeller motif. Here, we investigate by SPR the interactions between those two modules and the β‐propeller. Our results indicate that the two modules cooperate to bind the β‐propeller. The binding is favored by low pH and by high [Ca ++ ]. Our data show that Mg ++ , at high concentration in the endosome, favors the formation of the closed conformation by replacing the structuring effect of Ca ++ in LR5. We propose a sequential model of LDL release where formation of the close conformation follows LDL release.

10.1016/j.febslet.2015.10.014

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Citations (7)

Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation

Ramón Hurtado‐Guerrero Matilde de las Rivas

10.2210/pdb5ndf/pdb

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Glactose oxidase C383S mutant identified by directed evolution

D. Wilkinson N. Akumanyi Ramón Hurtado‐Guerrero H. Dawkes Peter F. Knowles

10.2210/pdb1t2x/pdb

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FERREDOXIN-NADP REDUCTASE (MUTATION S80A) COMPLEXED WITH NADP BY COCRYSTALLIZATION

Marta Martı́nez-Júlvez Ramón Hurtado‐Guerrero B. Herguedas A. Sanchez-Azqueta Manuel Hervás

Ferredoxin—NADP(+) reductase

10.2210/pdb3zc3/pdb

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Crystal structure of C. parvum GNA1 in complex with acetyl-CoA and glucose 6P.

Jacques Chi Marta Cova M. de las Rivas A. Medina Rafael J. Borges

Crystal (programming language)

10.2210/pdb6yug/pdb

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Synthesis and immunological evaluation of TLR1/2 ligand-conjugated RBDs as self-adjuvanting vaccine candidates against SARS-CoV-2

Chemical Communications (2024)

Yoshiyuki Manabe Brandon Gárate-Reyes Keita Ito Ramón Hurtado‐Guerrero Kazuya Kabayama

We synthesized and evaluated Pam 3 CSK 4 -conjugated receptor binding domain (RBD)/deglycosylated RBD as potential anti-severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) vaccine candidates.

10.1039/d4cc00462k

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Citations (1)

Dataset for "A Family of Di-Glutamate Mucin Degrading Enzymes that Bridges Glycan Hydrolases and Peptidases"

Zenodo (CERN European Organization for Nuclear Research) (2023)

Yoshiki Narimatsu Christian Büll Víctor Taleb Qinghua Liao Ismael Compañón

This dataset provides the classical and QM/MM MD simulation trajectory data to the manuscript: A Family of Di-Glutamate Mucin Degrading Enzymes that Bridges Glycan Hydrolases and Peptidases The data set contains classical MD simulations of HC7 with substrate peptides, thermodynamics integration (TI) simulations, as well as QM/MM OPES-explore simulations for our manuscript. PDB files for Figure 4f and Figure S21 are also included. A high resolution pdf file of Figure S28 is included, too.

10.5281/zenodo.10103923

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Substrate‐Guided Front‐Face Reaction Revealed by Combined Structural Snapshots and Metadynamics for the Polypeptide N‐Acetylgalactosaminyltransferase 2

Angewandte Chemie (2014)

Erandi Lira‐Navarrete Javier Iglesias‐Fernández Wesley F. Zandberg Ismael Compañón Yun Kong

Abstract The retaining glycosyltransferase GalNAc‐T2 is a member of a large family of human polypeptide GalNAc‐transferases that is responsible for the post‐translational modification of many cell‐surface proteins. By the use of combined structural and computational approaches, we provide the first set of structural snapshots of the enzyme during the catalytic cycle and combine these with quantum‐mechanics/molecular‐mechanics (QM/MM) metadynamics to unravel the catalytic mechanism of this retaining enzyme at the atomic‐electronic level of detail. Our study provides a detailed structural rationale for an ordered bi–bi kinetic mechanism and reveals critical aspects of substrate recognition, which dictate the specificity for acceptor Thr versus Ser residues and enforce a front‐face S N i‐type reaction in which the substrate N ‐acetyl sugar substituent coordinates efficient glycosyl transfer.

Metadynamics

QM/MM

10.1002/ange.201402781

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Citations (10)

Structure-Guided Approach for the Development of MUC1-Glycopeptide-Based Cancer Vaccines with Predictable Responses

JACS Au (2023)

Iris A. Bermejo Ana Guerreiro Ander Eguskiza Nuria Martínez‐Sáez Foivos S. Lazaris

Mucin-1 (MUC1) glycopeptides are exceptional candidates for potential cancer vaccines. However, their autoantigenic nature often results in a weak immune response. To overcome this drawback, we carefully engineered synthetic antigens with precise chemical modifications. To be effective and stimulate an anti-MUC1 response, artificial antigens must mimic the conformational dynamics of natural antigens in solution and have an equivalent or higher binding affinity to anti-MUC1 antibodies than their natural counterparts. As a proof of concept, we have developed a glycopeptide that contains noncanonical amino acid (2

MUC1

10.1021/jacsau.3c00587

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Citations (4)

bleached galactose oxidase

Melanie S. Rogers Ramón Hurtado‐Guerrero S.J. Firbank Malcolm A. Halcrow David M. Dooley

10.2210/pdb2vz3/pdb

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Citations (0)