1kl8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1kl8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kl8" /> '''NMR STRUCTURAL ANALYSIS OF THE COMPLEX FORME...)
Line 1: Line 1:
-
[[Image:1kl8.jpg|left|200px]]<br /><applet load="1kl8" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1kl8.jpg|left|200px]]<br /><applet load="1kl8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kl8" />
caption="1kl8" />
'''NMR STRUCTURAL ANALYSIS OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND THE PRINCIPAL ALPHA-NEUROTOXIN BINDING SEQUENCE ON THE ALPHA7 SUBUNIT OF A NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR'''<br />
'''NMR STRUCTURAL ANALYSIS OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND THE PRINCIPAL ALPHA-NEUROTOXIN BINDING SEQUENCE ON THE ALPHA7 SUBUNIT OF A NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR'''<br />
==Overview==
==Overview==
-
We report a new, higher resolution NMR structure of alpha-bungarotoxin, that defines the structure-determining disulfide core and beta-sheet, regions. We further report the NMR structure of the stoichiometric complex, formed between alpha-bungarotoxin and a recombinantly expressed 19-mer, peptide ((178)IPGKRTESFYECCKEPYPD(196)) derived from the alpha7 subunit of, the chick neuronal nicotinic acetylcholine receptor. A comparison of these, two structures reveals binding-induced stabilization of the flexible tip, of finger II in alpha-bungarotoxin. The conformational rearrangements in, the toxin create an extensive binding surface involving both sides of the, alpha7 19-mer hairpin-like structure. At the contact zone, Ala(7), Ser(9), and Ile(11) in finger I and Arg(36), Lys(38), Val(39), and Val(40) in, finger II of alpha-bungarotoxin interface with Phe(186), Tyr(187), Glu(188), and Tyr(194) in the alpha7 19-mer underscoring the importance of, receptor aromatic residues as critical neurotoxin-binding determinants., Superimposing the structure of the complex onto that of the, acetylcholine-binding protein (1I9B), a soluble homologue of the, extracellular domain of the alpha7 receptor, places alpha-bungarotoxin at, the peripheral surface of the inter-subunit interface occluding the, agonist-binding site. The disulfide-rich core of alpha-bungarotoxin is, suggested to be tilted in the direction of the membrane surface with, finger II extending into the proposed ligand-binding cavity.
+
We report a new, higher resolution NMR structure of alpha-bungarotoxin that defines the structure-determining disulfide core and beta-sheet regions. We further report the NMR structure of the stoichiometric complex formed between alpha-bungarotoxin and a recombinantly expressed 19-mer peptide ((178)IPGKRTESFYECCKEPYPD(196)) derived from the alpha7 subunit of the chick neuronal nicotinic acetylcholine receptor. A comparison of these two structures reveals binding-induced stabilization of the flexible tip of finger II in alpha-bungarotoxin. The conformational rearrangements in the toxin create an extensive binding surface involving both sides of the alpha7 19-mer hairpin-like structure. At the contact zone, Ala(7), Ser(9), and Ile(11) in finger I and Arg(36), Lys(38), Val(39), and Val(40) in finger II of alpha-bungarotoxin interface with Phe(186), Tyr(187), Glu(188), and Tyr(194) in the alpha7 19-mer underscoring the importance of receptor aromatic residues as critical neurotoxin-binding determinants. Superimposing the structure of the complex onto that of the acetylcholine-binding protein (1I9B), a soluble homologue of the extracellular domain of the alpha7 receptor, places alpha-bungarotoxin at the peripheral surface of the inter-subunit interface occluding the agonist-binding site. The disulfide-rich core of alpha-bungarotoxin is suggested to be tilted in the direction of the membrane surface with finger II extending into the proposed ligand-binding cavity.
==About this Structure==
==About this Structure==
-
1KL8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KL8 OCA].
+
1KL8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KL8 OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Basus, V.J.]]
+
[[Category: Basus, V J.]]
[[Category: Hawrot, E.]]
[[Category: Hawrot, E.]]
[[Category: Moise, L.]]
[[Category: Moise, L.]]
Line 25: Line 25:
[[Category: protein-peptide complex]]
[[Category: protein-peptide complex]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:20:27 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:21 2008''

Revision as of 11:35, 21 February 2008

Image:1kl8.jpg

1kl8

Drag the structure with the mouse to rotate

NMR STRUCTURAL ANALYSIS OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND THE PRINCIPAL ALPHA-NEUROTOXIN BINDING SEQUENCE ON THE ALPHA7 SUBUNIT OF A NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR

Overview

We report a new, higher resolution NMR structure of alpha-bungarotoxin that defines the structure-determining disulfide core and beta-sheet regions. We further report the NMR structure of the stoichiometric complex formed between alpha-bungarotoxin and a recombinantly expressed 19-mer peptide ((178)IPGKRTESFYECCKEPYPD(196)) derived from the alpha7 subunit of the chick neuronal nicotinic acetylcholine receptor. A comparison of these two structures reveals binding-induced stabilization of the flexible tip of finger II in alpha-bungarotoxin. The conformational rearrangements in the toxin create an extensive binding surface involving both sides of the alpha7 19-mer hairpin-like structure. At the contact zone, Ala(7), Ser(9), and Ile(11) in finger I and Arg(36), Lys(38), Val(39), and Val(40) in finger II of alpha-bungarotoxin interface with Phe(186), Tyr(187), Glu(188), and Tyr(194) in the alpha7 19-mer underscoring the importance of receptor aromatic residues as critical neurotoxin-binding determinants. Superimposing the structure of the complex onto that of the acetylcholine-binding protein (1I9B), a soluble homologue of the extracellular domain of the alpha7 receptor, places alpha-bungarotoxin at the peripheral surface of the inter-subunit interface occluding the agonist-binding site. The disulfide-rich core of alpha-bungarotoxin is suggested to be tilted in the direction of the membrane surface with finger II extending into the proposed ligand-binding cavity.

About this Structure

1KL8 is a Protein complex structure of sequences from Bungarus multicinctus and Gallus gallus. Full crystallographic information is available from OCA.

Reference

NMR structural analysis of alpha-bungarotoxin and its complex with the principal alpha-neurotoxin-binding sequence on the alpha 7 subunit of a neuronal nicotinic acetylcholine receptor., Moise L, Piserchio A, Basus VJ, Hawrot E, J Biol Chem. 2002 Apr 5;277(14):12406-17. Epub 2002 Jan 14. PMID:11790782

Page seeded by OCA on Thu Feb 21 13:35:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kl8"
Personal tools