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PDBsum entry 1ea3
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Influenza virus
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PDB id
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1ea3
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Combined results from solution studies on intact influenza virus m1 protein and from a new crystal form of its n-Terminal domain show that m1 is an elongated monomer.
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Authors
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S.Arzt,
F.Baudin,
A.Barge,
P.Timmins,
W.P.Burmeister,
R.W.Ruigrok.
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Ref.
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Virology, 2001,
279,
439-446.
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PubMed id
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Abstract
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The amino-terminal domain of influenza A virus matrix protein (residues 1-164)
was crystallized at pH 7 into a new crystal form in space group P1. This packing
of the protein implies that M1(1-164) was monomeric in solution when it
crystallized. Otherwise, the structure of the M1 fragment in the pH 7 crystals
was the same as the monomers in crystals formed at pH 4 where crystal packing
resulted in dimer formation [B. Sha and M. Luo, 1997, Nature Struct. Biol. 4,
239-244]. Analysis of intact M1 protein, the N-terminal domain, and the
remaining C-terminal fragment (residues 165-252) in solution also showed that
the N-terminal domain was monomeric with the same dimensions as determined from
the crystal structure. Intact M1 protein was also monomeric but with an
elongated shape due to the presence of the C-terminal part. Circular dichroism
showed that the C-terminal part of M1 contained helical structure. A model for
soluble M1 is presented, based on the assumption that the C-terminal domain is
spherical, in which the N- and C-terminal domains are connected by a linker
sequence which is available for proteolytic attack.
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