Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Freddy Poortmans"'
Autor:
Robert C. Liddington, Lode Wyns, Laurence Van Melderen, M.-H. Dao-Thi, Freddy Poortmans, El Mustapha Bahassi, Martine Couturier, Remy Loris
Publikováno v:
Journal of Molecular Biology. 285:1667-1677
The crystal structure of CcdB, a protein that poisons Escherichia coli gyrase, was determined in three crystal forms. The protein consists of a five-stranded antiparallel beta-pleated sheet followed by a C-terminal alpha-helix. In one of the loops of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a9712a184b8eab8baff95c1eab769eb8
https://doi.org/10.1006/jmbi.1998.2395
https://doi.org/10.1006/jmbi.1998.2395
Autor:
Remy Loris, Abdel Fattah Haikal, Ingrid Zegers, Jan Steyaert, Freddy Poortmans, Lode Wyns, Gillis Dehollander
Publikováno v:
Nature Structural Biology. 5:280-283
Here we present a time-resolved crystallographic analysis of the hydrolysis of exo (Sp) guanosine 2′,3′-cyclophosphoroth-ioate by RNase T1. The use of a slow substrate and fast crystallization methods made it possible to perform the study with co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::960fd601f3e7492d56cc12090c136f68
https://doi.org/10.1038/nsb0498-280
https://doi.org/10.1038/nsb0498-280
Autor:
Minh-Hoa Dao Thi, Mehdi Arbabi Ghahroudi, Thomas R. Transue, Raymond Hamers, Freddy Poortmans, Serge Muyldermans, Aline Desmyter, Lode Wyns
Publikováno v:
Nature Structural & Molecular Biology. 3:803-811
The Camelidae is the only taxonomic family known to possess functional heavy-chain antibodies, lacking light chains. We report here the 2.5 A resolution crystal structure of a camel VH in complex with its antigen, lysozyme. Compared to human and mous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6c3911a2d86fe069692cd79d2da3b89f
https://doi.org/10.1038/nsb0996-803
https://doi.org/10.1038/nsb0996-803
Publikováno v:
Journal of Biological Chemistry. 271:16144-16150
The lectin concanavalin A (ConA) sequentially binds a transition metal ion in the metal-binding site S1 and a calcium ion in the metal-binding site S2 to form its saccharide-binding site. Metal-free ConA crystals soaked with either Zn2+ (apoZn-ConA)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e807834e7b9de83d86494d89bd3589ae
https://doi.org/10.1074/jbc.271.27.16144
https://doi.org/10.1074/jbc.271.27.16144
Autor:
Freddy Poortmans, Thomas Hamelryck, Lode Wyns, M.-H. Dao-Thi, Toni A. Voelker, Maarten J. Chrispeels
Publikováno v:
Proteins: Structure, Function, and Genetics. 24:134-137
In the seeds of legume plants a class of sugar-binding proteins can be found, generally called legume lectins. In this paper we present the crystallization of phytohemagglutinin-L (PHA-L), a glycosylated lectin from the seeds of the common bean (Phas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9e0e9f62948915c93bdbe40bb7e3162
https://doi.org/10.1002/(sici)1097-0134(199601)24:1<134::aid-prot9>3.0.co
https://doi.org/10.1002/(sici)1097-0134(199601)24:1<134::aid-prot9>3.0.co
Publikováno v:
Proteins: Structure, Function, and Genetics. 20:330-346
The structures of two crystal forms of lentil lectin are determined and refined at high resolution. Orthorhombic lentil lectin is refined at 1.80 A resolution to anR-factor of 0.184 and monoclinic lentil lectin at 1.75 A resolution to anR-factor of 0
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b9d0a6b24f9ce2dd47bc66f6317626f
https://doi.org/10.1002/prot.340200406
https://doi.org/10.1002/prot.340200406
Publikováno v:
Protein Science. 3:2322-2339
The interactions of RNase A with cytidine 3'-monophosphate (3'-CMP) and deoxycytidyl-3',5'-deoxyadenosine (d(CpA)) were analyzed by X-ray crystallography. The 3'-CMP complex and the native structure were determined from trigonal crystals, and the d(C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e24dc331538e66fe3eed37df5de6f371
https://doi.org/10.1002/pro.5560031217
https://doi.org/10.1002/pro.5560031217
Autor:
Roger Pelle, Freddy Poortmans, Jan Steyaert, Noel B. Murphy, Thomas R. Transue, M.-H. Dao-Thi
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 54:1046-1048
Cyclophilin A from the bovine parasite Trypanosoma brucei brucei has been cloned, expressed in Escherichia coli, purified and crystallized in the presence of cyclosporin A using ammonium sulfate as a precipitant. The crystals belong to the orthorhomb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa6f450050501bfcb5b6b07af64d4c9c
https://doi.org/10.1107/s0907444998001607
https://doi.org/10.1107/s0907444998001607
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 52:879-881
Concanavalin A was co-crystallized in two crystal forms with 3,6-di-O-methyl- (alpha-D-mannopyranosyl) alpha- D-mannopyranoside, which is primarily responsible for the high-affinity binding of N-linked carbohydrates to concanavalin A. Both crystal fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfe2c2160ab6791487338f018f08abe6
https://doi.org/10.1107/s0907444996001953
https://doi.org/10.1107/s0907444996001953
The reversible binding of manganese and calcium to concanavalin A determines the carbohydrate binding of the lectin by inducing large conformational changes. These changes are governed by the isomerization of a non-proline peptide bond, Ala-207-Asp-2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5913dbad1a0b0b35b626161f5535f2a8
https://hdl.handle.net/20.500.14017/2902fbeb-f5e7-4fcf-9ca9-b06d41ca874f
https://hdl.handle.net/20.500.14017/2902fbeb-f5e7-4fcf-9ca9-b06d41ca874f
