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1.
15 p, 2.0 MB Identification of a novel polyfluorinated compound as a lead to inhibit human enzymes aldose reductase and AKR1B10 : structure determination of both ternary complexes and implications for drug design / Cousido-Siah, Alexandra (Institut de Génétique et de Biologie Moléculaire et Cellulaire (Illkirch, França)) ; Ruiz, Francesc X. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Mitschler, André (Institut de Génétique et de Biologie Moléculaire et Cellulaire (Illkirch, França)) ; Porte Orduna, Sergio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; De Lera, Ángel R. (Universidade de Vigo. Departamento de Quimica Orgánica) ; Martín, María J. (Parque Tecnológico de León. Biomar Microbial Technologies S.A.) ; Manzanaro, Sonia (Parque Tecnológico de León. Biomar Microbial Technologies S.A.) ; de la Fuente, Jesús A. (Parque Tecnológico de León. Biomar Microbial Technologies S.A.) ; Terwesten, Felix (Universität Marburg. Department of Pharmaceutical Chemistry) ; Betz, Michael (Universität Marburg. Department of Pharmaceutical Chemistry) ; Klebe, Gerhard (Universität Marburg. Department of Pharmaceutical Chemistry) ; Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Podjarny, Alberto (Institut de Génétique et de Biologie Moléculaire et Cellulaire (Illkirch, França))
Aldo-keto reductases (AKRs) are mostly monomeric enzymes which fold into a highly conserved ([alpha]/[beta])8 barrel, while their substrate specificity and inhibitor selectivity are determined by interaction with residues located in three highly variable external loops. [...]
2014 - 10.1107/S1399004713033452
Acta crystallographica. Section D, Biological crystallography, Vol. 70 (December 2014) , p. 889-903  
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2.
5 p, 495.2 KB Determination of hemihedral twinning and initial structural analysis of crystals of the procarboxypeptidase A ternary complex / Gomis-Rüth, F. Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Fita Rodríguez, Ignasi (Escola Tècnica Superior d'Enginyeria Industrial. Departament d'Enginyeria Química) ; Kiefersauer, R. (Max-Planck-Institut für Biochemie. Abteilung für Strukturforschung) ; Huber, Robert (Max-Planck-Institut für Biochemie. Abteilung für Strukturforschung) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Navaza, J. (Centre national de la recherche scientifique (França). Laboratoire de Physique)
The initial structural analysis of the ternary complex of procarboxypeptidase A from hemihedrally twinned crystals diffracting up to 2. 8 Å is described. Detection of twinning by different techniques is presented, including biochemical and intensity statistics approaches. [...]
1995 - 10.1107/S0907444995000643
Acta crystallographica. Section D, Biological crystallography, Vol. 51, Issue 5 (September 1995) , p. 819-823  
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3.
4 p, 372.8 KB Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi / Valencia, Eva (Institut de Biologia Molecular de Barcelona) ; Rosell i Febres, Albert (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Larroy Hernando, Carolina (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Biosca Vaqué, José Antonio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Fita Rodríguez, Ignasi (Institut de Biologia Molecular de Barcelona) ; Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Ochoa, Wendy F. (Institut de Biologia Molecular de Barcelona)
Different crystal forms diffracting to high resolution have been obtained for two NADP(H)-dependent alcohol dehydrogenases, members of the medium-chain dehydrogenase/reductase superfamily: ScADHVI from Saccharomyces cerevisiae and ADH8 from Rana perezi. [...]
2003 - 10.1107/S090744490201661X
Acta crystallographica. Section D, Biological crystallography, Vol. 59, Issue 2 (February 2003) , p. 334-337  
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4.
8 p, 1.0 MB Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid) / Pallarès i Goitiz, Irantzu (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Fernández Fleischhauer, Daniel (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Comellas-Bigler, Mireia (Max-Planck Institute of Biochemistry. Proteinase Research Group) ; Fernández-Recio, Juan (Barcelona Supercomputing Center) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Avilés, Francesc X. (Francesc Xavier) (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Bode, Wolfram (Max-Planck Institute of Biochemistry. Proteinase Research Group) ; Vendrell i Roca, Josep (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Carboxypeptidase A1 has been the subject of extensive research in the last 30 y and is one of the most widely studied zinc metalloenzymes. However, the three-dimensional structure of the human form of the enzyme is not yet available. [...]
2008 - 10.1107/S0907444908013474
Acta crystallographica. Section D, Biological crystallography, Vol. 64, Issue 7 (July 2008) , p. 784-791  
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