1kfh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kfh.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kfh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kfh| PDB=1kfh | SCENE= }}
{{STRUCTURE_1kfh| PDB=1kfh | SCENE= }}
-
'''Solution Structure of alpha-Bungarotoxin by NMR Spectroscopy'''
+
===Solution Structure of alpha-Bungarotoxin by NMR Spectroscopy===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11790782}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11790782 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11790782}}
==About this Structure==
==About this Structure==
-
1KFH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFH OCA].
+
1KFH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFH OCA].
==Reference==
==Reference==
Line 28: Line 32:
[[Category: Alpha-bungarotoxin]]
[[Category: Alpha-bungarotoxin]]
[[Category: Long snake neurotoxin]]
[[Category: Long snake neurotoxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:40:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:15:44 2008''

Revision as of 07:15, 2 July 2008

Image:1kfh.png

Template:STRUCTURE 1kfh

Solution Structure of alpha-Bungarotoxin by NMR Spectroscopy

Template:ABSTRACT PUBMED 11790782

About this Structure

1KFH is a Single protein structure of sequence from Bungarus multicinctus. Full experimental 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 Wed Jul 2 10:15:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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