A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction

Georges Mer; Maria Victoria Botuyan

doi:10.1016/j.str.2017.09.011

A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction

Georges Mer, Maria Victoria Botuyan

Biochemistry and Molecular Biology

Research output: Contribution to journal › Short survey › peer-review

1 Scopus citations

Abstract

Tandem BRCT domains are phophoprotein binding modules. In this issue of Structure, Sun et al. (2017) show that a single BRCT domain in TopBP1 binds tightly and specifically to phosphorylated Bloom syndrome helicase (BLM). This work reveals a novel BRCT binding mode and suggests a similar mechanism for TopBP1 interaction with 53BP1. Tandem BRCT domains are phophoprotein binding modules. In this issue of Structure, Sun et al. (2017) show that a single BRCT domain in TopBP1 binds tightly and specifically to phosphorylated Bloom syndrome helicase (BLM). This work reveals a novel BRCT binding mode and suggests a similar mechanism for TopBP1 interaction with 53BP1.

Original language	English (US)
Pages (from-to)	1471-1472
Number of pages	2
Journal	Structure
Volume	25
Issue number	10
DOIs	https://doi.org/10.1016/j.str.2017.09.011
State	Published - Oct 3 2017

ASJC Scopus subject areas

Structural Biology
Molecular Biology

Access to Document

10.1016/j.str.2017.09.011

Cite this

@article{44e7e5b76ef74ae0a8bc46e0304aa298,

title = "A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction",

abstract = "Tandem BRCT domains are phophoprotein binding modules. In this issue of Structure, Sun et al. (2017) show that a single BRCT domain in TopBP1 binds tightly and specifically to phosphorylated Bloom syndrome helicase (BLM). This work reveals a novel BRCT binding mode and suggests a similar mechanism for TopBP1 interaction with 53BP1. Tandem BRCT domains are phophoprotein binding modules. In this issue of Structure, Sun et al. (2017) show that a single BRCT domain in TopBP1 binds tightly and specifically to phosphorylated Bloom syndrome helicase (BLM). This work reveals a novel BRCT binding mode and suggests a similar mechanism for TopBP1 interaction with 53BP1.",

author = "Georges Mer and Botuyan, {Maria Victoria}",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd",

year = "2017",

month = oct,

day = "3",

doi = "10.1016/j.str.2017.09.011",

language = "English (US)",

volume = "25",

pages = "1471--1472",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "10",

}

TY - JOUR

T1 - A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction

AU - Mer, Georges

AU - Botuyan, Maria Victoria

PY - 2017/10/3

Y1 - 2017/10/3

N2 - Tandem BRCT domains are phophoprotein binding modules. In this issue of Structure, Sun et al. (2017) show that a single BRCT domain in TopBP1 binds tightly and specifically to phosphorylated Bloom syndrome helicase (BLM). This work reveals a novel BRCT binding mode and suggests a similar mechanism for TopBP1 interaction with 53BP1. Tandem BRCT domains are phophoprotein binding modules. In this issue of Structure, Sun et al. (2017) show that a single BRCT domain in TopBP1 binds tightly and specifically to phosphorylated Bloom syndrome helicase (BLM). This work reveals a novel BRCT binding mode and suggests a similar mechanism for TopBP1 interaction with 53BP1.

AB - Tandem BRCT domains are phophoprotein binding modules. In this issue of Structure, Sun et al. (2017) show that a single BRCT domain in TopBP1 binds tightly and specifically to phosphorylated Bloom syndrome helicase (BLM). This work reveals a novel BRCT binding mode and suggests a similar mechanism for TopBP1 interaction with 53BP1. Tandem BRCT domains are phophoprotein binding modules. In this issue of Structure, Sun et al. (2017) show that a single BRCT domain in TopBP1 binds tightly and specifically to phosphorylated Bloom syndrome helicase (BLM). This work reveals a novel BRCT binding mode and suggests a similar mechanism for TopBP1 interaction with 53BP1.

UR - http://www.scopus.com/inward/record.url?scp=85030460376&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85030460376&partnerID=8YFLogxK

U2 - 10.1016/j.str.2017.09.011

DO - 10.1016/j.str.2017.09.011

M3 - Short survey

C2 - 28978405

AN - SCOPUS:85030460376

SN - 0969-2126

VL - 25

SP - 1471

EP - 1472

JO - Structure

JF - Structure

IS - 10

ER -

A New BRCT Binding Mode in TopBP1-BLM Helicase Interaction

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this