1c9a

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(New page: 200px<br /> <applet load="1c9a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9a" /> '''SOLUTION STRUCTURE OF NEUROMEDIN B'''<br />...)
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<applet load="1c9a" size="450" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION STRUCTURE OF NEUROMEDIN B'''<br />
'''SOLUTION STRUCTURE OF NEUROMEDIN B'''<br />
==Overview==
==Overview==
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The solution structure of neuromedin B (NMB) was investigated using, two-dimensional nuclear magnetic resonance (NMR) spectroscopy in, membrane-mimicking environments. NMB adopts a relaxed helical conformation, from Trp(4) to Met(10) in 50% aqueous 2,2, 2-trifluoroethanol (TFE), solution and in 150 mM SDS micelles. Sidechain atoms of the three, residues, Trp(4), His(8) and Phe(9) orient toward the same direction and, these residues might play a key role on interacting with hydrophobic acyl, chains of the phospholipids in the membrane. NOESY experiments performed, on NMB in non-deuterated SDS micelle show that aromatic ring protons of, Trp(4) and Phe(9) residues are in close contact with methylene protons of, SDS micelles. In addition, proton longitudinal relaxation data proved that, the interactions between NMB with SDS micelle are characterized as, extrinsic interaction. Trp(4) and Phe(9) seem to be important in, interaction with receptor and this agrees with the previous studies of, structure-activity relationship (Howell, D.C. et al. (1996) Int. J. Pept., Protein Res. 48, 522-531). These conformational features might be helpful, in understanding the molecular mechanism of the function of NMB and, developing the efficient drugs.
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The solution structure of neuromedin B (NMB) was investigated using two-dimensional nuclear magnetic resonance (NMR) spectroscopy in membrane-mimicking environments. NMB adopts a relaxed helical conformation from Trp(4) to Met(10) in 50% aqueous 2,2, 2-trifluoroethanol (TFE) solution and in 150 mM SDS micelles. Sidechain atoms of the three residues, Trp(4), His(8) and Phe(9) orient toward the same direction and these residues might play a key role on interacting with hydrophobic acyl chains of the phospholipids in the membrane. NOESY experiments performed on NMB in non-deuterated SDS micelle show that aromatic ring protons of Trp(4) and Phe(9) residues are in close contact with methylene protons of SDS micelles. In addition, proton longitudinal relaxation data proved that the interactions between NMB with SDS micelle are characterized as extrinsic interaction. Trp(4) and Phe(9) seem to be important in interaction with receptor and this agrees with the previous studies of structure-activity relationship (Howell, D.C. et al. (1996) Int. J. Pept. Protein Res. 48, 522-531). These conformational features might be helpful in understanding the molecular mechanism of the function of NMB and developing the efficient drugs.
==About this Structure==
==About this Structure==
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1C9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C9A OCA].
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1C9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9A OCA].
==Reference==
==Reference==
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[[Category: peptide]]
[[Category: peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:18:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:03:46 2008''

Revision as of 10:03, 21 February 2008

Image:1c9a.gif

1c9a

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SOLUTION STRUCTURE OF NEUROMEDIN B

Overview

The solution structure of neuromedin B (NMB) was investigated using two-dimensional nuclear magnetic resonance (NMR) spectroscopy in membrane-mimicking environments. NMB adopts a relaxed helical conformation from Trp(4) to Met(10) in 50% aqueous 2,2, 2-trifluoroethanol (TFE) solution and in 150 mM SDS micelles. Sidechain atoms of the three residues, Trp(4), His(8) and Phe(9) orient toward the same direction and these residues might play a key role on interacting with hydrophobic acyl chains of the phospholipids in the membrane. NOESY experiments performed on NMB in non-deuterated SDS micelle show that aromatic ring protons of Trp(4) and Phe(9) residues are in close contact with methylene protons of SDS micelles. In addition, proton longitudinal relaxation data proved that the interactions between NMB with SDS micelle are characterized as extrinsic interaction. Trp(4) and Phe(9) seem to be important in interaction with receptor and this agrees with the previous studies of structure-activity relationship (Howell, D.C. et al. (1996) Int. J. Pept. Protein Res. 48, 522-531). These conformational features might be helpful in understanding the molecular mechanism of the function of NMB and developing the efficient drugs.

About this Structure

1C9A is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of neuromedin B by (1)H nuclear magnetic resonance spectroscopy., Lee S, Kim Y, FEBS Lett. 1999 Oct 29;460(2):263-9. PMID:10544247

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