2jnt

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(New page: 200px<br /><applet load="2jnt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jnt" /> '''Structure of Bombyx mori Chemosensory Protei...)
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==Overview==
==Overview==
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Chemosensory Proteins (CSPs) represent a family of conserved proteins, found in insects that may be involved in chemosensory functions. BmorCSP1, is expressed mainly in antennae and legs of the silkworm moth Bombyx mori, and was cloned from antennal cDNA. Here we report the determination of the, structure of Bombyx mori CSP1 (BmorCSP1) by NMR. The overall fold of, BmorCSP1 is globular and comprises six alpha-helices. These helices span, residues 10-14, 17-27, 35-49, 57-72, 75-85, and 92-100. The internal, hydrophobic sides of the helices are formed mostly by leucine and, isoleucine residues and, therefore, well suited to constitute a binding, site for hydrophobic ligands.
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Chemosensory Proteins (CSPs) represent a family of conserved proteins found in insects that may be involved in chemosensory functions. BmorCSP1 is expressed mainly in antennae and legs of the silkworm moth Bombyx mori and was cloned from antennal cDNA. Here we report the determination of the structure of Bombyx mori CSP1 (BmorCSP1) by NMR. The overall fold of BmorCSP1 is globular and comprises six alpha-helices. These helices span residues 10-14, 17-27, 35-49, 57-72, 75-85, and 92-100. The internal hydrophobic sides of the helices are formed mostly by leucine and isoleucine residues and, therefore, well suited to constitute a binding site for hydrophobic ligands.
==About this Structure==
==About this Structure==
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[[Category: ligand binding protein]]
[[Category: ligand binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:08:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:36 2008''

Revision as of 16:04, 21 February 2008


2jnt

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Structure of Bombyx mori Chemosensory Protein 1 in Solution

Overview

Chemosensory Proteins (CSPs) represent a family of conserved proteins found in insects that may be involved in chemosensory functions. BmorCSP1 is expressed mainly in antennae and legs of the silkworm moth Bombyx mori and was cloned from antennal cDNA. Here we report the determination of the structure of Bombyx mori CSP1 (BmorCSP1) by NMR. The overall fold of BmorCSP1 is globular and comprises six alpha-helices. These helices span residues 10-14, 17-27, 35-49, 57-72, 75-85, and 92-100. The internal hydrophobic sides of the helices are formed mostly by leucine and isoleucine residues and, therefore, well suited to constitute a binding site for hydrophobic ligands.

About this Structure

2JNT is a Single protein structure of sequence from Bombyx mori. Full crystallographic information is available from OCA.

Reference

Structure of Bombyx mori chemosensory protein 1 in solution., Jansen S, Chmelik J, Zidek L, Padrta P, Novak P, Zdrahal Z, Picimbon JF, Lofstedt C, Sklenar V, Arch Insect Biochem Physiol. 2007 Nov;66(3):135-45. PMID:17966128

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