1ea3
From Proteopedia
(New page: 200px<br /><applet load="1ea3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ea3, resolution 2.3Å" /> '''INFLUENZA VIRUS M1 PR...) |
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| - | [[Image:1ea3.jpg|left|200px]]<br /><applet load="1ea3" size=" | + | [[Image:1ea3.jpg|left|200px]]<br /><applet load="1ea3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ea3, resolution 2.3Å" /> | caption="1ea3, resolution 2.3Å" /> | ||
'''INFLUENZA VIRUS M1 PROTEIN'''<br /> | '''INFLUENZA VIRUS M1 PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The amino-terminal domain of influenza A virus matrix protein (residues | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1EA3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http:// | + | 1EA3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EA3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: matrix protein]] | [[Category: matrix protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:37 2008'' |
Revision as of 10:25, 21 February 2008
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INFLUENZA VIRUS M1 PROTEIN
Overview
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.
About this Structure
1EA3 is a Single protein structure of sequence from Influenza a virus. Full crystallographic information is available from OCA.
Reference
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., Arzt S, Baudin F, Barge A, Timmins P, Burmeister WP, Ruigrok RW, Virology. 2001 Jan 20;279(2):439-46. PMID:11162800
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