1ijc: Difference between revisions

Revision as of 12:19, 1 July 2008

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File:1ijc.png

Template:STRUCTURE 1ijc

Solution Structure of Bucandin, a Neurotoxin from the Venom of the Malayan KraitSolution Structure of Bucandin, a Neurotoxin from the Venom of the Malayan Krait

Template:ABSTRACT PUBMED 11736642

About this StructureAbout this Structure

1IJC is a Single protein structure of sequence from Bungarus candidus. Full experimental information is available from OCA.

ReferenceReference

NMR structure of bucandin, a neurotoxin from the venom of the Malayan krait (Bungarus candidus)., Torres AM, Kini RM, Selvanayagam N, Kuchel PW, Biochem J. 2001 Dec 15;360(Pt 3):539-48. PMID:11736642

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-'''Solution Structure of Bucandin, a Neurotoxin from the Venom of the Malayan Krait'''
+===Solution Structure of Bucandin, a Neurotoxin from the Venom of the Malayan Krait===
-==Overview==
+<!--
-A high-resolution solution structure of bucandin, a neurotoxin from Malayan krait (Bungarus candidus), was determined by (1)H-NMR spectroscopy and molecular dynamics. The average backbone root-mean-square deviation for the 20 calculated structures and the mean structure is 0.47 A (1 A=0.1 nm) for all residues and 0.24 A for the well-defined region that spans residues 23-58. Secondary-structural elements include two antiparallel beta-sheets characterized by two and four strands. According to recent X-ray analysis, bucandin adopts a typical three-finger loop motif and yet it has some peculiar characteristics that set it apart from other common alpha-neurotoxins. The presence of a fourth strand in the second antiparallel beta-sheet had not been observed before in three-finger toxins, and this feature was well represented in the NMR structure. Although the overall fold of the NMR structure is similar to that of the X-ray crystal structure, there are significant differences between the two structures that have implications for the pharmacological action of the toxin. These include the extent of the beta-sheets, the conformation of the region spanning residues 42-49 and the orientation of some side chains. In comparison with the X-ray structure, the NMR structure shows that the hydrophobic side chains of Trp(27) and Trp(36) are stacked together and are orientated towards the tip of the middle loop. The NMR study also showed that the two-stranded beta-sheet incorporated in the first loop, as defined by residues 1-22, and the C-terminus from Asn(59), is probably flexible relative to the rest of the molecule. On the basis of the dispositions of the hydrophobic and hydrophilic side chains, the structure of bucandin is clearly different from those of cytotoxins.
+The line below this paragraph, {{ABSTRACT_PUBMED_11736642}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11736642 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11736642}}
 ==About this Structure==
-IJC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bungarus_candidus Bungarus candidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJC OCA].
+IJC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bungarus_candidus Bungarus candidus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJC OCA].
 ==Reference==
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 [[Category: Two and four stranded beta-sheet]]
 [[Category: Two antiparallel beta-sheet]]
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