Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association

Kook Han Kim, Seung Kon Hong, Kwang Yeon Hwang, Eunice Eunkyeong Kim

Research output: Contribution to journalArticle

Abstract

Muskelin is an intracellular kelch-repeat protein comprised of discoidin, LisH, CTLH and kelch-repeat domains. It is involved in cell adhesion and the regulation of cytoskeleton dynamics as well as being a component of a putative E3 ligase complex. Here, the first crystal structure of mouse muskelin discoidin domain (MK-DD) is reported at 1.55 Å resolution, which reveals a distorted eight-stranded β-barrel with two short α-helices at one end of the barrel. Interestingly, the N- and C-termini are not linked by the disulfide bonds found in other eukaryotic discoidin structures. A highly conserved MIND motif appears to be the determinant for MK-DD specific interaction together with the spike loops. Analysis of interdomain interaction shows that MK-DD binds the kelch-repeat domain directly and that this interaction depends on the presence of the LisH domain.

Original languageEnglish
Pages (from-to)2863-2874
Number of pages12
JournalActa Crystallographica Section D: Biological Crystallography
Volume70
Issue number11
DOIs
Publication statusPublished - 2014 Jan 1

Fingerprint

Ubiquitin-Protein Ligases
Cytoskeleton
Cell Adhesion
Disulfides
Kelch Repeat
Discoidin Domain
Proteins

Cite this

Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association. / Kim, Kook Han; Hong, Seung Kon; Hwang, Kwang Yeon; Kim, Eunice Eunkyeong.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 70, No. 11, 01.01.2014, p. 2863-2874.

Research output: Contribution to journalArticle

@article{a0261f10a36a4c339be9bb0d1c0bc214,
title = "Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association",
abstract = "Muskelin is an intracellular kelch-repeat protein comprised of discoidin, LisH, CTLH and kelch-repeat domains. It is involved in cell adhesion and the regulation of cytoskeleton dynamics as well as being a component of a putative E3 ligase complex. Here, the first crystal structure of mouse muskelin discoidin domain (MK-DD) is reported at 1.55 {\AA} resolution, which reveals a distorted eight-stranded β-barrel with two short α-helices at one end of the barrel. Interestingly, the N- and C-termini are not linked by the disulfide bonds found in other eukaryotic discoidin structures. A highly conserved MIND motif appears to be the determinant for MK-DD specific interaction together with the spike loops. Analysis of interdomain interaction shows that MK-DD binds the kelch-repeat domain directly and that this interaction depends on the presence of the LisH domain.",
keywords = "CTLH complex, discoidin domain, kelch repeat, muskelin, self-association",
author = "Kim, {Kook Han} and Hong, {Seung Kon} and Hwang, {Kwang Yeon} and Kim, {Eunice Eunkyeong}",
year = "2014",
month = "1",
day = "1",
doi = "10.1107/S139900471401894X",
language = "English",
volume = "70",
pages = "2863--2874",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "11",

}

TY - JOUR

T1 - Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association

AU - Kim, Kook Han

AU - Hong, Seung Kon

AU - Hwang, Kwang Yeon

AU - Kim, Eunice Eunkyeong

PY - 2014/1/1

Y1 - 2014/1/1

N2 - Muskelin is an intracellular kelch-repeat protein comprised of discoidin, LisH, CTLH and kelch-repeat domains. It is involved in cell adhesion and the regulation of cytoskeleton dynamics as well as being a component of a putative E3 ligase complex. Here, the first crystal structure of mouse muskelin discoidin domain (MK-DD) is reported at 1.55 Å resolution, which reveals a distorted eight-stranded β-barrel with two short α-helices at one end of the barrel. Interestingly, the N- and C-termini are not linked by the disulfide bonds found in other eukaryotic discoidin structures. A highly conserved MIND motif appears to be the determinant for MK-DD specific interaction together with the spike loops. Analysis of interdomain interaction shows that MK-DD binds the kelch-repeat domain directly and that this interaction depends on the presence of the LisH domain.

AB - Muskelin is an intracellular kelch-repeat protein comprised of discoidin, LisH, CTLH and kelch-repeat domains. It is involved in cell adhesion and the regulation of cytoskeleton dynamics as well as being a component of a putative E3 ligase complex. Here, the first crystal structure of mouse muskelin discoidin domain (MK-DD) is reported at 1.55 Å resolution, which reveals a distorted eight-stranded β-barrel with two short α-helices at one end of the barrel. Interestingly, the N- and C-termini are not linked by the disulfide bonds found in other eukaryotic discoidin structures. A highly conserved MIND motif appears to be the determinant for MK-DD specific interaction together with the spike loops. Analysis of interdomain interaction shows that MK-DD binds the kelch-repeat domain directly and that this interaction depends on the presence of the LisH domain.

KW - CTLH complex

KW - discoidin domain

KW - kelch repeat

KW - muskelin

KW - self-association

UR - http://www.scopus.com/inward/record.url?scp=84908622925&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84908622925&partnerID=8YFLogxK

U2 - 10.1107/S139900471401894X

DO - 10.1107/S139900471401894X

M3 - Article

VL - 70

SP - 2863

EP - 2874

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 11

ER -