1omb: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1omb.gif|left|200px]]
{{Seed}}
[[Image:1omb.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1omb|  PDB=1omb  |  SCENE=  }}  
{{STRUCTURE_1omb|  PDB=1omb  |  SCENE=  }}  


'''SEQUENTIAL ASSIGNMENT AND STRUCTURE DETERMINATION OF SPIDER TOXIN OMEGA-AGA-IVB'''
===SEQUENTIAL ASSIGNMENT AND STRUCTURE DETERMINATION OF SPIDER TOXIN OMEGA-AGA-IVB===




==Overview==
<!--
The solution structure of a peptide toxin isolated from funnel web spider venom, omega-Aga-IVB, was determined by 2D NMR methods. omega-Aga-IVB is a high-affinity specific blocker of P-type voltage-dependent calcium channels. Nearly all of the proton resonances of this 48-residue protein were assigned using conventional 2D homonuclear NMR experiments. The three-dimensional structure of the molecule was determined by simulated annealing. The distance and dihedral restraints used in the structure calculations were derived from NOESY and COSY-type experiments, respectively. Mass spectrometric analysis of omega-Aga-IVB suggests that the protein contains four disulfide bonds. In the absence of chemical data to identify the pattern of cysteine pairing, the disulfide bonds of the toxin are proposed from the NMR data and subsequent structural calculations. The structure of the toxin can be described as a three-stranded anti-parallel beta sheet connected by flexible loops. A striking feature of the structure is that the C-terminal 10 residues of this protein adopt random coil conformations. Several positively charged amino acid side chains are found localized on one face of the molecule, in close proximity to the C-terminal tail. This observation has led us to propose a speculative model of the toxins blockade mechanism.
The line below this paragraph, {{ABSTRACT_PUBMED_8241166}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8241166 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8241166}}


==About this Structure==
==About this Structure==
1OMB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agelenopsis_aperta Agelenopsis aperta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMB OCA].  
1OMB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agelenopsis_aperta Agelenopsis aperta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMB OCA].  


==Reference==
==Reference==
Line 26: Line 30:
[[Category: Yu, H.]]
[[Category: Yu, H.]]
[[Category: Toxin]]
[[Category: Toxin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:01:33 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:57:43 2008''

Revision as of 22:57, 27 July 2008

File:1omb.png

Template:STRUCTURE 1omb

SEQUENTIAL ASSIGNMENT AND STRUCTURE DETERMINATION OF SPIDER TOXIN OMEGA-AGA-IVB

Template:ABSTRACT PUBMED 8241166

About this Structure

1OMB is a Single protein structure of sequence from Agelenopsis aperta. Full experimental information is available from OCA.

Reference

Sequential assignment and structure determination of spider toxin omega-Aga-IVB., Yu H, Rosen MK, Saccomano NA, Phillips D, Volkmann RA, Schreiber SL, Biochemistry. 1993 Dec 7;32(48):13123-9. PMID:8241166

Page seeded by OCA on Mon Jul 28 01:57:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1omb&oldid=675607"