1mi2

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(New page: 200px<br /><applet load="1mi2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mi2" /> '''SOLUTION STRUCTURE OF MURINE MACROPHAGE INFL...)
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'''SOLUTION STRUCTURE OF MURINE MACROPHAGE INFLAMMATORY PROTEIN-2, NMR, 20 STRUCTURES'''<br />
'''SOLUTION STRUCTURE OF MURINE MACROPHAGE INFLAMMATORY PROTEIN-2, NMR, 20 STRUCTURES'''<br />
==Overview==
==Overview==
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The solution structure of murine macrophage inflammatory protein-2, (MIP-2), a heparin-binding chemokine that is secreted in response to, inflammatory stimuli, has been determined using two-dimensional, homonuclear and heteronuclear NMR spectroscopy. Structure calculations, were carried out by means of torsion-angle molecular dynamics using the, program X-PLOR. The structure is based on a total of 2390 experimental, restraints, comprising 2246 NOE-derived distance restraints, 44 distance, restraints for 22 hydrogen bonds, and 100 torsion angle restraints. The, structure is well-defined, with the backbone (N, Calpha, C) and heavy atom, atomic rms distribution about the mean coordinates for residues 9-69 of, the dimer being 0.57 +/- 0.16 A and 0.96 +/- 0.12 A, respectively. The N-, and C-terminal residues (1-8 and 70-73, respectively) are disordered. The, overall structure of the MIP-2 dimer is similar to that reported, previously for the NMR structures of MGSA and IL-8 and consists of a, six-stranded antiparallel beta-sheet (residue 25-29, 39-44, and 48-52), packed against two C-terminal antiparallel alpha-helices. A best fit, superposition of the NMR structure of MIP-2 on the structures of MGSA, NAP-2, and the NMR and X-ray structures of IL-8 are 1.11, 1.02, 1.27, and, 1.19 A, respectively, for the monomers, and 1.28, 1.10, 1.55, and 1.36 A, respectively, for the dimers (IL-8 residues 7-14 and 16-67, NAP-2 residues, 25-84). At the tertiary level, the main differences between the MIP-2, solution structure and the IL-8, MGSA, and NAP-2 structures involve the, N-terminal loop between residues 9-23 and the loops formed by residues, 30-38 and residues 53-58. At the quaternary level, the difference between, MIP-2 and IL-8, MGSA, or NAP-2 results from differing interhelical angles, and separations.
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The solution structure of murine macrophage inflammatory protein-2 (MIP-2), a heparin-binding chemokine that is secreted in response to inflammatory stimuli, has been determined using two-dimensional homonuclear and heteronuclear NMR spectroscopy. Structure calculations were carried out by means of torsion-angle molecular dynamics using the program X-PLOR. The structure is based on a total of 2390 experimental restraints, comprising 2246 NOE-derived distance restraints, 44 distance restraints for 22 hydrogen bonds, and 100 torsion angle restraints. The structure is well-defined, with the backbone (N, Calpha, C) and heavy atom atomic rms distribution about the mean coordinates for residues 9-69 of the dimer being 0.57 +/- 0.16 A and 0.96 +/- 0.12 A, respectively. The N- and C-terminal residues (1-8 and 70-73, respectively) are disordered. The overall structure of the MIP-2 dimer is similar to that reported previously for the NMR structures of MGSA and IL-8 and consists of a six-stranded antiparallel beta-sheet (residue 25-29, 39-44, and 48-52) packed against two C-terminal antiparallel alpha-helices. A best fit superposition of the NMR structure of MIP-2 on the structures of MGSA, NAP-2, and the NMR and X-ray structures of IL-8 are 1.11, 1.02, 1.27, and 1.19 A, respectively, for the monomers, and 1.28, 1.10, 1.55, and 1.36 A, respectively, for the dimers (IL-8 residues 7-14 and 16-67, NAP-2 residues 25-84). At the tertiary level, the main differences between the MIP-2 solution structure and the IL-8, MGSA, and NAP-2 structures involve the N-terminal loop between residues 9-23 and the loops formed by residues 30-38 and residues 53-58. At the quaternary level, the difference between MIP-2 and IL-8, MGSA, or NAP-2 results from differing interhelical angles and separations.
==About this Structure==
==About this Structure==
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1MI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MI2 OCA].
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1MI2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI2 OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Jerva, L.F.]]
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[[Category: Jerva, L F.]]
[[Category: Lolis, E.]]
[[Category: Lolis, E.]]
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[[Category: Schweitzer, B.I.]]
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[[Category: Schweitzer, B I.]]
[[Category: Shao, W.]]
[[Category: Shao, W.]]
[[Category: West, J.]]
[[Category: West, J.]]
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[[Category: nmr]]
[[Category: nmr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:25:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:21 2008''

Revision as of 11:55, 21 February 2008

Image:1mi2.gif

1mi2

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SOLUTION STRUCTURE OF MURINE MACROPHAGE INFLAMMATORY PROTEIN-2, NMR, 20 STRUCTURES

Overview

The solution structure of murine macrophage inflammatory protein-2 (MIP-2), a heparin-binding chemokine that is secreted in response to inflammatory stimuli, has been determined using two-dimensional homonuclear and heteronuclear NMR spectroscopy. Structure calculations were carried out by means of torsion-angle molecular dynamics using the program X-PLOR. The structure is based on a total of 2390 experimental restraints, comprising 2246 NOE-derived distance restraints, 44 distance restraints for 22 hydrogen bonds, and 100 torsion angle restraints. The structure is well-defined, with the backbone (N, Calpha, C) and heavy atom atomic rms distribution about the mean coordinates for residues 9-69 of the dimer being 0.57 +/- 0.16 A and 0.96 +/- 0.12 A, respectively. The N- and C-terminal residues (1-8 and 70-73, respectively) are disordered. The overall structure of the MIP-2 dimer is similar to that reported previously for the NMR structures of MGSA and IL-8 and consists of a six-stranded antiparallel beta-sheet (residue 25-29, 39-44, and 48-52) packed against two C-terminal antiparallel alpha-helices. A best fit superposition of the NMR structure of MIP-2 on the structures of MGSA, NAP-2, and the NMR and X-ray structures of IL-8 are 1.11, 1.02, 1.27, and 1.19 A, respectively, for the monomers, and 1.28, 1.10, 1.55, and 1.36 A, respectively, for the dimers (IL-8 residues 7-14 and 16-67, NAP-2 residues 25-84). At the tertiary level, the main differences between the MIP-2 solution structure and the IL-8, MGSA, and NAP-2 structures involve the N-terminal loop between residues 9-23 and the loops formed by residues 30-38 and residues 53-58. At the quaternary level, the difference between MIP-2 and IL-8, MGSA, or NAP-2 results from differing interhelical angles and separations.

About this Structure

1MI2 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Solution structure of murine macrophage inflammatory protein-2., Shao W, Jerva LF, West J, Lolis E, Schweitzer BI, Biochemistry. 1998 Jun 9;37(23):8303-13. PMID:9622482

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