Výsledky vyhledávání - "T L, Blundell"

Crystal structure of an Xrcc4-DNA ligase IV complex

Autor: B L, Sibanda, S E, Critchlow, J, Begun, X Y, Pei, S P, Jackson, T L, Blundell, L, Pellegrini

Publikováno v: Nature structural biology. 8(12)

A complex of two proteins, Xrcc4 and DNA ligase IV, plays a fundamental role in DNA non-homologous end joining (NHEJ), a cellular function required for double-strand break repair and V(D)J recombination. Here we report the crystal structure of human

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d3b96abcfdc79bae2cb265dfe9c559e8
https://pubmed.ncbi.nlm.nih.gov/11702069

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FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties

Autor: J, Shi, T L, Blundell, K, Mizuguchi

Publikováno v: Journal of molecular biology. 310(1)

FUGUE, a program for recognizing distant homologues by sequence-structure comparison (http://www-cryst.bioc.cam.ac.uk/fugue/), has three key features. (1) Improved environment-specific substitution tables. Substitutions of an amino acid in a protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::605582bff758f16eba3defeb674a9f2b
https://pubmed.ncbi.nlm.nih.gov/11419950

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Incorporating knowledge-based biases into an energy-based side-chain modeling method: application to comparative modeling of protein structure

Autor: J, Mendes, H A, Nagarajaram, C M, Soares, T L, Blundell, M A, Carrondo

Publikováno v: Biopolymers. 59(2)

The performance of the self-consistent mean field theory (SCMFT) method for side-chain modeling, employing rotamer energies calculated with the flexible rotamer model (FRM), is evaluated in the context of comparative modeling of protein structure. Pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6a8d1dfc381ab626fdfccda97d18cc14
https://pubmed.ncbi.nlm.nih.gov/11373721

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A novel exhaustive search algorithm for predicting the conformation of polypeptide segments in proteins

Autor: C M, Deane, T L, Blundell

Publikováno v: Proteins. 40(1)

We present a fast ab initio method for the prediction of local conformations in proteins. The program, PETRA, selects polypeptide fragments from a computer-generated database (APD) encoding all possible peptide fragments up to twelve amino acids long

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e9042a52da5a975b10c353c220b7bf85
https://pubmed.ncbi.nlm.nih.gov/10813838

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An iterative structure-assisted approach to sequence alignment and comparative modeling

Autor: D F, Burke, C M, Deane, H A, Nagarajaram, N, Campillo, M, Martin-Martinez, J, Mendes, F, Molina, J, Perry, B V, Reddy, C M, Soares, R E, Steward, M, Williams, M A, Carrondo, T L, Blundell, K, Mizuguchi

Publikováno v: Proteins.

Correct alignment of the sequence of a target protein with those of homologues of known three-dimensional structure is a key step in comparative modeling. Usually an iterative approach that takes account of the local and overall structural features i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e3ede26b6818ff100de2ad1a9d01f19f
https://pubmed.ncbi.nlm.nih.gov/10526352

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Interactions of protein kinase CK2 subunits

Autor: I, Korn, S, Gutkind, N, Srinivasan, T L, Blundell, C C, Allende, J E, Allende

Publikováno v: Molecular and cellular biochemistry. 191(1-2)

Several approaches have been used to study the interactions of the subunits of protein kinase CK2. The inactive mutant of CK2alpha that has Asp 156 mutated to Ala (CK2alphaA156) is able to bind the CK2beta subunit and to compete effectively in this b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::07f4ad17de416b12e462f1b91ed50e35
https://pubmed.ncbi.nlm.nih.gov/10094395

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Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding

Autor: D Y, Chirgadze, J P, Hepple, H, Zhou, R A, Byrd, T L, Blundell, E, Gherardi

Publikováno v: Nature structural biology. 6(1)

Although ligand-induced receptor dimerization is a common prerequisite for receptor activation, the mode by which different growth factors bind their receptors and cause them to dimerize varies considerably. Here we report the crystal structure at 2.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2a57ee3ce4e2f43c849bcfa361632574
https://pubmed.ncbi.nlm.nih.gov/9886295

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Sequence and structure conservation in a protein core

Autor: M A, Rodionov, T L, Blundell

Publikováno v: Proteins. 33(3)

In order to study structural aspects of sequence conservation in families of homologous proteins, we have analyzed structurally aligned sequences of 585 proteins grouped into 128 homologous families. The conservation of a residue in a family is defin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9aa1b06f6b8f9ce82a229522eea3fde4
https://pubmed.ncbi.nlm.nih.gov/9829695

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