This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1fsc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fsc.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fsc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fsc| PDB=1fsc | SCENE= }}
{{STRUCTURE_1fsc| PDB=1fsc | SCENE= }}
-
'''CRYSTAL STRUCTURE OF FASCICULIN 2 FROM GREEN MAMBA SNAKE VENOM: EVIDENCE FOR UNUSUAL LOOP FLEXIBILITY'''
+
===CRYSTAL STRUCTURE OF FASCICULIN 2 FROM GREEN MAMBA SNAKE VENOM: EVIDENCE FOR UNUSUAL LOOP FLEXIBILITY===
-
==Overview==
+
<!--
-
The crystal structure of the snake toxin fasciculin 2, a potent acetylcholinesterase inhibitor from the venom of the green mamba (Dendroaspis angusticeps), has been determined by the molecular-replacement method, using the fasciculin 1 model and refined to 2.0 A resolution. The introduction of an overall anisotropic temperature factor improved significantly the quality of the electron-density map. It suggests, as it was also indicated by the packing, that the thermal motion along the unique axis direction is less pronounced than on the (ab) plane. The final crystallographic R factor is 0.188 for a model having r.m.s. deviations from ideality of 0.016 A for bond lengths and 2.01 degrees for bond angles. As fasciculin 1, fasciculin 2 belongs to the three-finger class of Elapidae toxins, a structural group that also contains the alpha-neurotoxins and the cardiotoxins. Although the two fasciculins have, overall, closely related structures, the conformation of loop I differs appreciably in the two molecules. The presence of detergent in crystallization medium in the case of fasciculin 2 appears to be responsible for the displacement of the loop containing Thr9. This conformational change also results in the formation of a crystallographic dimer that displays extensive intermolecular interactions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299729}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299729 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299729}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Housset, D.]]
[[Category: Housset, D.]]
[[Category: Snake toxin]]
[[Category: Snake toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:42:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:52:21 2008''

Revision as of 00:52, 1 July 2008

Image:1fsc.png

Template:STRUCTURE 1fsc

CRYSTAL STRUCTURE OF FASCICULIN 2 FROM GREEN MAMBA SNAKE VENOM: EVIDENCE FOR UNUSUAL LOOP FLEXIBILITY

Template:ABSTRACT PUBMED 15299729

About this Structure

1FSC is a Single protein structure of sequence from Dendroaspis angusticeps. Full crystallographic information is available from OCA.

Reference

Structure of fasciculin 2 from green mamba snake venom: evidence for unusual loop flexibility., le Du MH, Housset D, Marchot P, Bougis PE, Navaza J, Fontecilla-Camps JC, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):87-92. PMID:15299729

Page seeded by OCA on Tue Jul 1 03:52:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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