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Structure of the regulatory subunit of CK2 in the presence of a p21WAF1peptide demonstrates flexibility of the acidic loop

Autor: V. Dhanaraj, Jorge E. Allende, Muhammed Sayed, Xue-Yuan Pei, Loic Bertrand, Tom L. Blundell, Emilio Parisini, Victor M. Bolanos-Garcia

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 60:1698-1704

A truncated form of the regulatory subunit of the protein kinase CK2beta (residues 1-178) has been crystallized in the presence of a fragment of the cyclin-dependent kinase inhibitor p21WAF1 (residues 46-65) and the structure solved at 2.9 A resoluti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9d9d599a7010832358928270ea25ea9
https://doi.org/10.1107/s0907444904016750

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Cockroach Allergen Bla g 2

Autor: Tom L. Blundell, Anna Pomés, V. Dhanaraj, Lisa D. Vailes, Martin D. Chapman

Publikováno v: American Journal of Respiratory and Critical Care Medicine. 165:391-397

Exposure to German cockroach (Blattella germanica) allergens is associated with the development of chronic respiratory diseases, especially asthma. The mechanism by which allergic patients develop specific immunoglobulin E (IgE) responses to environm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::187f8bf61834bddb239b61d53569021e
https://doi.org/10.1164/ajrccm.165.3.2104027

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A six-stranded double-psi β barrel is shared by several protein superfamilies

Autor: Armando Albert, V. Dhanaraj, Tom L. Blundell, Richard M Castillo, Alexey G. Murzin, Kenji Mizuguchi

Publikováno v: Structure. 7:227-236

Background: Six-stranded β barrels with a pseudo-twofold axis are found in several proteins. One group comprises a Greek-key structure with all strands antiparallel; an example is the N-terminal domain of ferredoxin reductase. Others involve paralle

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0dc56b427a80d659b18fefab62688eb5
https://doi.org/10.1016/s0969-2126(99)80028-8

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X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: Implications for inhibitor selectivity

Autor: Alexander Pavlovsky, Claude Forsey Purchase, V. Dhanaraj, Bruce D. Roth, Donald Hupe, Mark G. Williams, Ye Qi-Zhuang, Christine Humblet, Tom L. Blundell, Daniel F. Ortwine, Andrew D. White, Johnson Linda Lea

Publikováno v: Protein Science. 8:1455-1462

Effective inhibitors of matrix metalloproteinases (MMPs), a family of connective tissue-degrading enzymes, could be useful for the treatment of diseases such as cancer, multiple sclerosis, and arthritis. Many of the known MMP inhibitors are derived f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6be3c2dd98f451553f22e2be953b531e
https://doi.org/10.1110/ps.8.7.1455

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A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure

Autor: Dennis J. Hoover, Mohammed O. Badasso, Philip Nugent, Tom L. Blundell, V. Dhanaraj, J. E. Pitts, Matthew Groves

Publikováno v: University of Groningen
Protein Engineering, 11(10), 833-840

In the crystal structure of uncomplexed native chymosin, the beta-hairpin at the active site, known as 'the flap', adopts a different conformation from that of other aspartic proteinases. This conformation would prevent the mode of binding of substra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fee8fd6d169af041c07b6f849fe8896
https://doi.org/10.1093/protein/11.10.833

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Crystal structure of aspartate decarboxylase at 2.2 Å resolution provides evidence for an ester in protein self–processing

Autor: B. L. Sibanda, Armando Albert, Manoj K. Ramjee, Alison G. Smith, Tom L. Blundell, G. Khan, F. von Delft, Ulrich Genschel, V. Dhanaraj, Michael Witty, R. Pulido, Chris Abell

Publikováno v: Nature Structural Biology. 5:289-293

The structure of L-aspartate-alpha-decarboxylase from E. coli has been determined at 2.2 A resolution. The enzyme is a tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1b70b0378c3e9ace3e04272614a30e7
https://doi.org/10.1038/nsb0498-289

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X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily

Autor: Alexander Pavlovsky, V. Dhanaraj, Daniel F. Ortwine, James B. Dunbar, Ye Qi-Zhuang, Johnson Linda Lea, J. R. Rubin, Donald Hupe, Christine Humblet, Tom L. Blundell

Publikováno v: Structure. 4:375-386

Background: Stromelysin belongs to a family of zinc-dependent endopeptidases referred to as matrix metalloproteinases (MMPs, matrixins) because of their capacity for selective degradation of various components of the extracellular matrix. Matrixins p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ff5b0e15e9a8dfbce80fa9821d8b694
https://doi.org/10.1016/s0969-2126(96)00043-3

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Protein engineering loops in aspartic proteinases: site-directed mutagenesis, biochemical characterization and X-ray analysis of chymosin with a replaced loop from rhizopuspepsin

Autor: P. Orprayoon, Phil Nugent, J. E. Pitts, Julie Wilsher, Tom L. Blundell, Armando Albert, V. Dhanaraj

Publikováno v: Scopus-Elsevier

The loop exchange mutant chymosin 155-164 rhizopuspepsin was expressed in Trichoderma reesei and exported into the medium to yield a correctly folded and active product. The biochemical characterization and crystal structure determination at 2.5 A re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5c59104fe75d048a96195b734b3c27a
https://doi.org/10.1093/protein/9.10.885

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