Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
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Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 μ homology domainStructural basis for the binding of tryptophan-based motifs by δ-COP.δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function.9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.
P2860
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
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2015 թուականի Յունիսին հրատարակուած գիտական յօդուած
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2015 թվականի հունիսին հրատարակված գիտական հոդված
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
@zh-hk
2015年論文
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2015年論文
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2015年论文
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Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@ast
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@en
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@nl
type
label
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@ast
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@en
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@nl
prefLabel
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@ast
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@en
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@nl
P2093
P2860
P1476
Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution
@en
P2093
Anna Parnis
Avital Lahav
Dan Cassel
P2860
P304
P356
10.1107/S1399004715006203
P577
2015-06-01T00:00:00Z