Mutation of a critical tryptophan to lysine in avidin or streptavidin may explain why sea urchin fibropellin adopts an avidin-like domain.
about
Structural elements responsible for conversion of streptavidin to a pseudoenzymeChicken genome analysis reveals novel genes encoding biotin-binding proteins related to avidin family.Avidin related protein 2 shows unique structural and functional features among the avidin protein family.Chicken avidin exhibits pseudo-catalytic properties. Biochemical, structural, and electrostatic consequencesLigand exchange between proteins. Exchange of biotin and biotin derivatives between avidin and streptavidinDimer-Tetramer Transition between Solution and Crystalline States of Streptavidin and Avidin MutantsTamavidins--novel avidin-like biotin-binding proteins from the Tamogitake mushroomStructural and functional characteristics of xenavidin, the first frog avidin from Xenopus tropicalisStructural Adaptation of a Thermostable Biotin-binding Protein in a Psychrophilic EnvironmentZebavidin - An Avidin-Like Protein from ZebrafishDynamic partitioning of a glycosyl-phosphatidylinositol-anchored protein in glycosphingolipid-rich microdomains imaged by single-quantum dot tracking.Engineered single-chain dimeric streptavidins with an unexpected strong preference for biotin-4-fluoresceinEngineering soluble monomeric streptavidin with reversible biotin binding capability.Rendezvin: An essential gene encoding independent, differentially secreted egg proteins that organize the fertilization envelope proteome after self-associationChallenging semi-bootstrapping molecular-replacement strategy reveals intriguing crystal packing of rhizavidin.Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding.Enhancing the thermal stability of avidin. Introduction of disulfide bridges between subunit interfaces.Mutations for decreasing the immunogenicity and maintaining the function of core streptavidin.Chicken avidin-related proteins show altered biotin-binding and physico-chemical properties as compared with avidin.Mutation of the important Tyr-33 residue of chicken avidin: functional and structural consequencesAn avidin-like domain that does not bind biotin is adopted for oligomerization by the extracellular mosaic protein fibropellinEfficient production of active chicken avidin using a bacterial signal peptide in Escherichia coli.Characterization of poultry egg-white avidins and their potential as a tool in pretargeting cancer treatment.Biotin induces tetramerization of a recombinant monomeric avidin. A model for protein-protein interactions.Development and characterization of a series of soluble tetrameric and monomeric streptavidin muteins with differential biotin binding affinities.Rational design of an active avidin monomer.Single and multiple bonds in (strept)avidin-biotin interactions.Structure-based rational design of streptavidin mutants with pseudo-catalytic activity.Chicken avidin-related protein 4/5 shows superior thermal stability when compared with avidin while retaining high affinity to biotin.Construction of a dual chain pseudotetrameric chicken avidin by combining two circularly permuted avidins.Design and construction of highly stable, protease-resistant chimeric avidins.Novel avidin-like protein from a root nodule symbiotic bacterium, Bradyrhizobium japonicum.
P2860
Q24568056-0CAFB122-1746-445D-A94B-63ACB48C1A74Q24805137-042F6E97-8964-485C-838B-F4F378783CFCQ24816540-2AA6A071-ADA3-4DF3-A2C6-13F7CF3C12FDQ27632382-1BA8DD7E-13E0-4DB6-915F-1897F3D225DEQ27639140-7B5AD5F5-688F-4D9C-8890-E9DC7CCC9108Q27641582-4F07094A-9717-4254-B2C3-885E2082F6D0Q27653625-63D19982-C028-4432-B2E3-4D286EE56068Q27657606-B2531D5F-1D15-499D-A366-A26DA148CC3BQ27678441-8D943898-E541-41CF-A96A-E33153203EBFQ27680554-38B8255A-8E4C-44DC-9863-67DEB5C6140FQ30491186-6ACC4492-5667-432C-A915-9872BE7713FAQ33216583-48526F63-3EB2-4941-A006-27DD0D928670Q34412508-52439F7D-37D1-4D60-8E5E-01AE4761B1BAQ35191004-402180B0-0856-470D-A79C-F97DD20C6D49Q39969148-2F97E823-E26D-4E3A-93FF-9990EBD3F852Q40607406-915DCA76-C10B-4527-9604-308E890D4F2FQ40688035-C24312E4-2D7B-4851-8021-F26C8D8F3356Q41583623-F514E0F8-C854-4F08-8DBC-A56B20040F97Q42051740-5ED16E7F-1DB7-4B64-8B7F-9814B51328D2Q42099351-86A622DD-915A-43BD-8C56-911899DB6817Q42282488-E2F81ACE-0534-41BA-B101-2FB86F3222D9Q42808844-DBECEAF9-3775-468E-AD76-6A19FCE2322BQ43002836-315A2930-09A1-459E-A7B1-6E88B90794B9Q43509778-5F6C90B8-738B-4712-AD99-A8724A99319FQ43754786-1635522D-F56E-4A70-BA89-7F7D68F14705Q44233703-7852EFC5-5426-43B4-A324-3FF5E07BA3A5Q44253993-F1EC8872-7818-4898-9E61-8E004AA4EA5BQ44257226-5A354101-B813-4DFC-8835-9BB46BACD497Q44683467-D602E72C-88FA-4C0C-A33D-B1D5812F75D3Q44886641-48EA21B0-CCAD-41CC-9FD2-3433ED9DBB34Q45223558-03F01541-C932-49AF-BDE9-BBAD78F38544Q45254066-EAB2EA45-AE1E-4A3F-B2F3-002E91996D8B
P2860
Mutation of a critical tryptophan to lysine in avidin or streptavidin may explain why sea urchin fibropellin adopts an avidin-like domain.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Mutation of a critical tryptop ...... adopts an avidin-like domain.
@en
Mutation of a critical tryptop ...... adopts an avidin-like domain.
@nl
type
label
Mutation of a critical tryptop ...... adopts an avidin-like domain.
@en
Mutation of a critical tryptop ...... adopts an avidin-like domain.
@nl
prefLabel
Mutation of a critical tryptop ...... adopts an avidin-like domain.
@en
Mutation of a critical tryptop ...... adopts an avidin-like domain.
@nl
P2093
P2860
P1433
P1476
Mutation of a critical tryptop ...... n adopts an avidin-like domain
@en
P2093
A T Marttila
K J Airenne
M S Kulomaa
P2860
P356
10.1016/S0014-5793(99)01423-4
P407
P577
1999-11-01T00:00:00Z