1snd: Difference between revisions

Revision as of 09:42, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1snd.png

Template:STRUCTURE 1snd

STAPHYLOCOCCAL NUCLEASE DIMER CONTAINING A DELETION OF RESIDUES 114-119 COMPLEXED WITH CALCIUM CHLORIDE AND THE COMPETITIVE INHIBITOR DEOXYTHYMIDINE-3',5'-DIPHOSPHATESTAPHYLOCOCCAL NUCLEASE DIMER CONTAINING A DELETION OF RESIDUES 114-119 COMPLEXED WITH CALCIUM CHLORIDE AND THE COMPETITIVE INHIBITOR DEOXYTHYMIDINE-3',5'-DIPHOSPHATE

Template:ABSTRACT PUBMED 7552745

About this StructureAbout this Structure

1SND is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

One-step evolution of a dimer from a monomeric protein., Green SM, Gittis AG, Meeker AK, Lattman EE, Nat Struct Biol. 1995 Sep;2(9):746-51. PMID:7552745

Page seeded by OCA on Mon Jul 28 09:42:27 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1snd.gif|left|200px]]
+{{Seed}}
+[[Image:1snd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1snd|  PDB=1snd  |  SCENE=  }}
-'''STAPHYLOCOCCAL NUCLEASE DIMER CONTAINING A DELETION OF RESIDUES 114-119 COMPLEXED WITH CALCIUM CHLORIDE AND THE COMPETITIVE INHIBITOR DEOXYTHYMIDINE-3',5'-DIPHOSPHATE'''
+===STAPHYLOCOCCAL NUCLEASE DIMER CONTAINING A DELETION OF RESIDUES 114-119 COMPLEXED WITH CALCIUM CHLORIDE AND THE COMPETITIVE INHIBITOR DEOXYTHYMIDINE-3',5'-DIPHOSPHATE===
-==Overview==
+<!--
-Deletion of six amino acids in a surface loop transforms staphylococcal nuclease from a monomeric protein into a very stable dimer (Kd &lt; 1 x 10(-8)M). A 2 A X-ray crystal structure of the dimer (R = 0.176) shows that the carboxy-terminal alpha-helix has been stripped from its normal position in one monomer and is now incorporated into the equivalent position on the adjoining monomer. This swapping creates an association interface of 2900 A 2. A second, smaller interface of 460 A 2 is also formed. The spontaneous exchange or swapping of secondary structural elements provides a simple pathway for the formation of large, stable protein/protein interfaces and may play an important role in the evolution of oligomeric proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_7552745}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7552745 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7552745}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Nuclease]]
 [[Category: Signal]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:55:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:42:27 2008''