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 language | English |
|---|---|
| Pages (from-to) | 2863-2874 |
| Number of pages | 12 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 70 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2014 Jan 1 |
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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 journal › Article
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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 -