A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity. - Wikidata - awgldk - TriplyDB

A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

http://www.wikidata.org/entity/Q37434554

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Compound heterozygous mutation of Rag1 leading to Omenn syndrome Crystal structure of the V(D)J recombinase RAG1-RAG2 Elucidating the domain architecture and functions of non-core RAG1: the capacity of a non-core zinc-binding domain to function in nuclear import and nucleic acid binding Spatio-temporal regulation of RAG2 following genotoxic stress.Structural characterization of the second intra-discal loop of the photoreceptor tetraspanin RDS Riches in RAGs: Revealing the V(D)J Recombinase through High-Resolution Structures.New insights into the evolutionary origins of the recombination-activating gene proteins and V(D)J recombination.An interdomain boundary in RAG1 facilitates cooperative binding to RAG2 in formation of the V(D)J recombinase complex.Recombination-activating gene 1 and 2 (RAG1 and RAG2) in flounder (Paralichthys olivaceus).

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A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

http://www.wikidata.org/entity/Q37434554

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article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 03 June 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

@en

A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

@nl

type

label

A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

@en

A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

@nl

prefLabel

A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

@en

A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

@nl

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J.JMB.2009.05.076

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Journal of Molecular Biology

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A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.

@en

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Karla K Rodgers

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Lori M Gwyn

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Mandy M Peak

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Negar S Rahman

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Pallabi De

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P2860

RAG1 core and V(D)J recombination signal sequences were derived from Transib transposons

Amino acid residues in RAG1 responsible for the interaction with RAG2 during the V(D)J recombination process

V(D)J recombination: modulation of RAG1 and RAG2 cleavage activity on 12/23 substrates by whole cell extract and DNA-bending proteins

An ancient evolutionary origin of the Rag1/2 gene locus

The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2

Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis

Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster

The RAG proteins and V(D)J recombination: complexes, ends, and transposition

Putting the pieces together: identification and characterization of structural domains in the V(D)J recombination protein RAG1

Structure of thermolysin refined at 1.6 A resolution

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863-878

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scholarly article

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10.1016/J.JMB.2009.05.076

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2009-06-03T00:00:00Z

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19500590

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2782368

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