Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy

Yoon Hun Hong; Hee Chul Ahn; Jongsoo Lim; Hong Man Kim; Hye Young Ji; Seunga Lee; Ji Hun Kim; Eun Young Park; Hyun Kyu Song; Bong Jin Lee

doi:10.1016/j.febslet.2008.12.034

Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy

Yoon Hun Hong, Hee Chul Ahn, Jongsoo Lim, Hong Man Kim, Hye Young Ji, Seunga Lee, Ji Hun Kim, Eun Young Park, Hyun Kyu Song, Bong Jin Lee

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

Interaction between the signal-transducing adapter molecule 1 (STAM1) Vps27/Hrs/Stam (VHS) domain and ubiquitin was investigated by nuclear magnetic resonance (NMR) spectroscopy. NMR evidence showed that the structure of STAM1 VHS domain resembles that of other VHS domains, especially the homologous domain of STAM2. We found that the VHS domain binds to ubiquitin via its hydrophobic patch consisting of N-terminus of helix 2 and C-terminus of helix 4 in which Trp26 on helix 2 plays a pivotal role in the binding. The binding between VHS and ubiquitin seems to be very similar to that between ubiquitin associated domain (UBA) and ubiquitin, however, the direction of α-helices involved in the ubiquitin binding is opposite. Here, we propose a novel ubiquitin binding site and the manner of ubiquitin recognition of the STAM1 VHS domain. Structured summary: MINT-6804185:. STAM1 (uniprotkb:Q92783) binds (MI:0407) to ubiquitin (uniprotkb:P62988) by nuclear magnetic resonance (MI:0077).

Original language	English
Pages (from-to)	287-292
Number of pages	6
Journal	FEBS Letters
Volume	583
Issue number	2
DOIs	https://doi.org/10.1016/j.febslet.2008.12.034
Publication status	Published - 2009 Jan 22

Bibliographical note

Funding Information:
We thank the staff at the KIST 900 MHz NMR facility. This work was supported by a grant from the Basic Research Program of Korea Science and Engineering Foundation (R01-2004-000-10773-0). This work was also supported in part by the 2007 BK21 project for Medicine, Dentistry and Pharmacy, and by Grant 2Z03130 from Korea Institute of Science and Technology, Korea.

Keywords

Chemical shift perturbation
NMR spectroscopy
Protein-protein interaction
STAM1 VHS domain
Ubiquitin recognition

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2008.12.034

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title = "Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy",

abstract = "Interaction between the signal-transducing adapter molecule 1 (STAM1) Vps27/Hrs/Stam (VHS) domain and ubiquitin was investigated by nuclear magnetic resonance (NMR) spectroscopy. NMR evidence showed that the structure of STAM1 VHS domain resembles that of other VHS domains, especially the homologous domain of STAM2. We found that the VHS domain binds to ubiquitin via its hydrophobic patch consisting of N-terminus of helix 2 and C-terminus of helix 4 in which Trp26 on helix 2 plays a pivotal role in the binding. The binding between VHS and ubiquitin seems to be very similar to that between ubiquitin associated domain (UBA) and ubiquitin, however, the direction of α-helices involved in the ubiquitin binding is opposite. Here, we propose a novel ubiquitin binding site and the manner of ubiquitin recognition of the STAM1 VHS domain. Structured summary: MINT-6804185:. STAM1 (uniprotkb:Q92783) binds (MI:0407) to ubiquitin (uniprotkb:P62988) by nuclear magnetic resonance (MI:0077).",

keywords = "Chemical shift perturbation, NMR spectroscopy, Protein-protein interaction, STAM1 VHS domain, Ubiquitin recognition",

author = "Hong, {Yoon Hun} and Ahn, {Hee Chul} and Jongsoo Lim and Kim, {Hong Man} and Ji, {Hye Young} and Seunga Lee and Kim, {Ji Hun} and Park, {Eun Young} and Song, {Hyun Kyu} and Lee, {Bong Jin}",

note = "Funding Information: We thank the staff at the KIST 900 MHz NMR facility. This work was supported by a grant from the Basic Research Program of Korea Science and Engineering Foundation (R01-2004-000-10773-0). This work was also supported in part by the 2007 BK21 project for Medicine, Dentistry and Pharmacy, and by Grant 2Z03130 from Korea Institute of Science and Technology, Korea.",

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doi = "10.1016/j.febslet.2008.12.034",

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AU - Hong, Yoon Hun

AU - Ahn, Hee Chul

AU - Lim, Jongsoo

AU - Kim, Hong Man

AU - Ji, Hye Young

AU - Lee, Seunga

AU - Kim, Ji Hun

AU - Park, Eun Young

AU - Song, Hyun Kyu

AU - Lee, Bong Jin

N1 - Funding Information: We thank the staff at the KIST 900 MHz NMR facility. This work was supported by a grant from the Basic Research Program of Korea Science and Engineering Foundation (R01-2004-000-10773-0). This work was also supported in part by the 2007 BK21 project for Medicine, Dentistry and Pharmacy, and by Grant 2Z03130 from Korea Institute of Science and Technology, Korea.

PY - 2009/1/22

Y1 - 2009/1/22

N2 - Interaction between the signal-transducing adapter molecule 1 (STAM1) Vps27/Hrs/Stam (VHS) domain and ubiquitin was investigated by nuclear magnetic resonance (NMR) spectroscopy. NMR evidence showed that the structure of STAM1 VHS domain resembles that of other VHS domains, especially the homologous domain of STAM2. We found that the VHS domain binds to ubiquitin via its hydrophobic patch consisting of N-terminus of helix 2 and C-terminus of helix 4 in which Trp26 on helix 2 plays a pivotal role in the binding. The binding between VHS and ubiquitin seems to be very similar to that between ubiquitin associated domain (UBA) and ubiquitin, however, the direction of α-helices involved in the ubiquitin binding is opposite. Here, we propose a novel ubiquitin binding site and the manner of ubiquitin recognition of the STAM1 VHS domain. Structured summary: MINT-6804185:. STAM1 (uniprotkb:Q92783) binds (MI:0407) to ubiquitin (uniprotkb:P62988) by nuclear magnetic resonance (MI:0077).

AB - Interaction between the signal-transducing adapter molecule 1 (STAM1) Vps27/Hrs/Stam (VHS) domain and ubiquitin was investigated by nuclear magnetic resonance (NMR) spectroscopy. NMR evidence showed that the structure of STAM1 VHS domain resembles that of other VHS domains, especially the homologous domain of STAM2. We found that the VHS domain binds to ubiquitin via its hydrophobic patch consisting of N-terminus of helix 2 and C-terminus of helix 4 in which Trp26 on helix 2 plays a pivotal role in the binding. The binding between VHS and ubiquitin seems to be very similar to that between ubiquitin associated domain (UBA) and ubiquitin, however, the direction of α-helices involved in the ubiquitin binding is opposite. Here, we propose a novel ubiquitin binding site and the manner of ubiquitin recognition of the STAM1 VHS domain. Structured summary: MINT-6804185:. STAM1 (uniprotkb:Q92783) binds (MI:0407) to ubiquitin (uniprotkb:P62988) by nuclear magnetic resonance (MI:0077).

KW - Chemical shift perturbation

KW - NMR spectroscopy

KW - Protein-protein interaction

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KW - Ubiquitin recognition

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Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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