Structural insights into the recognition of phosphopeptide by the FHA domain of kanadaptin

Qingping Xu; Marc C Deller; Tine K Nielsen; Joanna C Grant; Scott A Lesley; Marc-André Elsliger; Ashley M Deacon; Ian A Wilson

doi:10.1371/journal.pone.0107309

Structural insights into the recognition of phosphopeptide by the FHA domain of kanadaptin

Qingping Xu, Marc C Deller, Tine K Nielsen, Joanna C Grant, Scott A Lesley, Marc-André Elsliger, Ashley M Deacon, Ian A Wilson

6 Citations (Scopus)

Abstract

Kanadaptin is a nuclear protein of unknown function that is widely expressed in mammalian tissues. The crystal structure of the forkhead-associated (FHA) domain of human kanadaptin was determined to 1.6 A˚resolution. The structure reveals an asymmetric dimer in which one monomer is complexed with a phosphopeptide mimic derived from a peptide segment from the N-terminus of a symmetry-related molecule as well as a sulfate bound to the structurally conserved phosphothreonine recognition cleft. This structure provides insights into the molecular recognition features utilized by this family of proteins and represents the first evidence that kanadaptin is likely involved in a phosphorylation-mediated signaling pathway. These results will be of use for designing experiments to further probe the function of kanadaptin.

Original language	English
Article number	e107309
Journal	PLOS ONE
Volume	9
Issue number	9
Number of pages	9
ISSN	1932-6203
DOIs	https://doi.org/10.1371/journal.pone.0107309
Publication status	Published - 8 Sept 2014

Access to Document

10.1371/journal.pone.0107309

Cite this

@article{a176b7e0fe194e68bc6f79ee550002f9,

title = "Structural insights into the recognition of phosphopeptide by the FHA domain of kanadaptin",

abstract = "Kanadaptin is a nuclear protein of unknown function that is widely expressed in mammalian tissues. The crystal structure of the forkhead-associated (FHA) domain of human kanadaptin was determined to 1.6 A˚resolution. The structure reveals an asymmetric dimer in which one monomer is complexed with a phosphopeptide mimic derived from a peptide segment from the N-terminus of a symmetry-related molecule as well as a sulfate bound to the structurally conserved phosphothreonine recognition cleft. This structure provides insights into the molecular recognition features utilized by this family of proteins and represents the first evidence that kanadaptin is likely involved in a phosphorylation-mediated signaling pathway. These results will be of use for designing experiments to further probe the function of kanadaptin.",

author = "Qingping Xu and Deller, {Marc C} and Nielsen, {Tine K} and Grant, {Joanna C} and Lesley, {Scott A} and Marc-Andr{\'e} Elsliger and Deacon, {Ashley M} and Wilson, {Ian A}",

year = "2014",

month = sep,

day = "8",

doi = "10.1371/journal.pone.0107309",

language = "English",

volume = "9",

journal = "PLoS Computational Biology",

issn = "1932-6203",

publisher = "Public Library of Science",

number = "9",

}

TY - JOUR

T1 - Structural insights into the recognition of phosphopeptide by the FHA domain of kanadaptin

AU - Xu, Qingping

AU - Deller, Marc C

AU - Nielsen, Tine K

AU - Grant, Joanna C

AU - Lesley, Scott A

AU - Elsliger, Marc-André

AU - Deacon, Ashley M

AU - Wilson, Ian A

PY - 2014/9/8

Y1 - 2014/9/8

N2 - Kanadaptin is a nuclear protein of unknown function that is widely expressed in mammalian tissues. The crystal structure of the forkhead-associated (FHA) domain of human kanadaptin was determined to 1.6 A˚resolution. The structure reveals an asymmetric dimer in which one monomer is complexed with a phosphopeptide mimic derived from a peptide segment from the N-terminus of a symmetry-related molecule as well as a sulfate bound to the structurally conserved phosphothreonine recognition cleft. This structure provides insights into the molecular recognition features utilized by this family of proteins and represents the first evidence that kanadaptin is likely involved in a phosphorylation-mediated signaling pathway. These results will be of use for designing experiments to further probe the function of kanadaptin.

AB - Kanadaptin is a nuclear protein of unknown function that is widely expressed in mammalian tissues. The crystal structure of the forkhead-associated (FHA) domain of human kanadaptin was determined to 1.6 A˚resolution. The structure reveals an asymmetric dimer in which one monomer is complexed with a phosphopeptide mimic derived from a peptide segment from the N-terminus of a symmetry-related molecule as well as a sulfate bound to the structurally conserved phosphothreonine recognition cleft. This structure provides insights into the molecular recognition features utilized by this family of proteins and represents the first evidence that kanadaptin is likely involved in a phosphorylation-mediated signaling pathway. These results will be of use for designing experiments to further probe the function of kanadaptin.

U2 - 10.1371/journal.pone.0107309

DO - 10.1371/journal.pone.0107309

M3 - Journal article

C2 - 25197798

SN - 1932-6203

VL - 9

JO - PLoS Computational Biology

JF - PLoS Computational Biology

IS - 9

M1 - e107309

ER -

Structural insights into the recognition of phosphopeptide by the FHA domain of kanadaptin

Abstract

Access to Document

Fingerprint

Cite this