1c9a

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[[Image:1c9a.gif|left|200px]]
[[Image:1c9a.gif|left|200px]]
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{{Structure
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|PDB= 1c9a |SIZE=350|CAPTION= <scene name='initialview01'>1c9a</scene>
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The line below this paragraph, containing "STRUCTURE_1c9a", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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{{STRUCTURE_1c9a| PDB=1c9a | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9a OCA], [http://www.ebi.ac.uk/pdbsum/1c9a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c9a RCSB]</span>
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'''SOLUTION STRUCTURE OF NEUROMEDIN B'''
'''SOLUTION STRUCTURE OF NEUROMEDIN B'''
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==About this Structure==
==About this Structure==
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1C9A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9A OCA].
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1C9A is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9A OCA].
==Reference==
==Reference==
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[[Category: Kim, Y.]]
[[Category: Kim, Y.]]
[[Category: Lee, S.]]
[[Category: Lee, S.]]
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[[Category: neuromedin b]]
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[[Category: Neuromedin b]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: peptide]]
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[[Category: Peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:29:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:17:18 2008''
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Revision as of 09:29, 2 May 2008

Image:1c9a.gif

Template:STRUCTURE 1c9a

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. 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 Page seeded by OCA on Fri May 2 12:29:22 2008

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