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PDBsum entry 1rfa
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Serine/threonine-protein kinase
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PDB id
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1rfa
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References listed in PDB file
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Key reference
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Title
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Solution structure of the ras-Binding domain of c-Raf-1 and identification of its ras interaction surface.
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Authors
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S.D.Emerson,
V.S.Madison,
R.E.Palermo,
D.S.Waugh,
J.E.Scheffler,
K.L.Tsao,
S.E.Kiefer,
S.P.Liu,
D.C.Fry.
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Ref.
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Biochemistry, 1995,
34,
6911-6918.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the Ras-binding domain of human c-Raf-1 (residues 55-132) has
been determined in solution by nuclear magnetic resonance (NMR) spectroscopy.
Following complete assignment of the backbone and side-chain 1H, 15N, and 13C
resonances, the structure was calculated using the program CHARMM. Over 1300
NOE-derived constraints were applied, resulting in a detailed structure. The
fold of Raf55-132 consists of a five-stranded beta-sheet, a 12-residue
alpha-helix, and an additional one-turn helix. It is similar to those of
ubiquitin and the IgG-binding domain of protein G, although the three proteins
share very little sequence identity. The surface of Raf55-132 that interacts
with Ras has been identified by monitoring perturbation of line widths and
chemical shifts of 15N-labeled Raf55-132 resonances during titration with
unlabeled Ras-GMPPNP. The Ras-binding site is contained within a spatially
contiguous patch comprised of the N-terminal beta-hairpin and the C-terminal end
of the alpha-helix.
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Secondary reference #1
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Title
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Chemical shift assignments and folding topology of the ras-Binding domain of human raf-1 as determined by heteronuclear three-Dimensional nmr spectroscopy.
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Authors
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S.D.Emerson,
D.S.Waugh,
J.E.Scheffler,
K.L.Tsao,
K.M.Prinzo,
D.C.Fry.
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Ref.
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Biochemistry, 1994,
33,
7745-7752.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Characterization of a 78-Residue fragment of c-Raf-1 that comprises a minimal binding domain for the interaction with ras-Gtp.
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Authors
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J.E.Scheffler,
D.S.Waugh,
E.Bekesi,
S.E.Kiefer,
J.E.Losardo,
A.Neri,
K.M.Prinzo,
K.L.Tsao,
B.Wegrzynski,
S.D.Emerson.
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Ref.
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J Biol Chem, 1994,
269,
22340-22346.
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PubMed id
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