1clp: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1clp.gif|left|200px]]
{{Seed}}
[[Image:1clp.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1clp|  PDB=1clp  |  SCENE=  }}  
{{STRUCTURE_1clp|  PDB=1clp  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF A CALCIUM-INDEPENDENT PHOSPHOLIPASELIKE MYOTOXIC PROTEIN FROM BOTHROPS ASPER VENOM'''
===CRYSTAL STRUCTURE OF A CALCIUM-INDEPENDENT PHOSPHOLIPASELIKE MYOTOXIC PROTEIN FROM BOTHROPS ASPER VENOM===




==Overview==
<!--  
Myotoxin II, a myotoxic calcium-independent phospholipase-like protein isolated from the venom of Bothrops asper, possesses no detectable phospholipase activity. The crystal structure has been determined and refined at 2.8 A to an R-factor of 16.5% (F &gt; 3sigma) with excellent stereochemistry. Amino-acid differences between catalytically active phospholipases and myotoxin II in the Ca(2+)-binding region, specifically the substitutions Tyr28--&gt;Asn, Gly32--&gt;Leu and Asp49--&gt;Lys, result in an altered local conformation. The key difference is that the epsilon-amino group of Lys49 fills the site normally occupied by the calcium ion in catalytically active phospholipases. In contrast to the homologous monomeric Lys49 variant from Agkistrodon piscivorus piscivorus, myotoxin II is present as a dimer both in solution and in the crystalline state. The two molecules in the asymmetric unit are related by a nearly perfect twofold axis, yet the dimer is radically different from the dimer formed by the phospholipase from Crotalus atrox. Whereas in C. atrox the dimer interface occludes the active sites, in myotoxin II they are exposed to solvent.
The line below this paragraph, {{ABSTRACT_PUBMED_15299297}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15299297 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15299297}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Ward, R J.]]
[[Category: Ward, R J.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:52:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:55:18 2008''

Revision as of 17:55, 30 June 2008

File:1clp.png

Template:STRUCTURE 1clp

CRYSTAL STRUCTURE OF A CALCIUM-INDEPENDENT PHOSPHOLIPASELIKE MYOTOXIC PROTEIN FROM BOTHROPS ASPER VENOM

Template:ABSTRACT PUBMED 15299297

About this Structure

1CLP is a Single protein structure of sequence from Bothrops asper. Full crystallographic information is available from OCA.

Reference

Structure of a calcium-independent phospholipase-like myotoxic protein from Bothrops asper venom., Arni RK, Ward RJ, Gutierrez JM, Tulinsky A, Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):311-7. PMID:15299297

Page seeded by OCA on Mon Jun 30 20:55:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1clp&oldid=583215"