5lve: Difference between revisions

Revision as of 14:05, 3 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:5lve.png

Template:STRUCTURE 5lve

STRUCTURE OF THE VARIABLE DOMAIN OF HUMAN IMMUNOGLOBULIN K-4 LIGHT CHAIN LENSTRUCTURE OF THE VARIABLE DOMAIN OF HUMAN IMMUNOGLOBULIN K-4 LIGHT CHAIN LEN

Template:ABSTRACT PUBMED 11045631

About this StructureAbout this Structure

5LVE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Change in dimerization mode by removal of a single unsatisfied polar residue located at the interface., Pokkuluri PR, Cai X, Johnson G, Stevens FJ, Schiffer M, Protein Sci. 2000 Sep;9(9):1852-5. PMID:11045631

Page seeded by OCA on Thu Jul 3 14:05:42 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:5lve.gif|left|200px]]
+{{Seed}}
+[[Image:5lve.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_5lve|  PDB=5lve  |  SCENE=  }}
-'''STRUCTURE OF THE VARIABLE DOMAIN OF HUMAN IMMUNOGLOBULIN K-4 LIGHT CHAIN LEN'''
+===STRUCTURE OF THE VARIABLE DOMAIN OF HUMAN IMMUNOGLOBULIN K-4 LIGHT CHAIN LEN===
-==Overview==
+<!--
-The importance of unsatisfied hydrogen bonding potential on protein-protein interaction was studied. Two alternate modes of dimerization (conventional and flipped form) of an immunoglobulin light chain variable domain (V(L)) were previously identified. In the flipped form, interface residue Gln89 would have an unsatisfied hydrogen bonding potential. Removal of this Gln should render the flipped dimer as the more favorable quaternary form. High resolution crystallographic studies of the Q89A and Q89L mutants show, as we predicted, that these proteins indeed form flipped dimers with very similar interfaces. A small cavity is present in the Q89A mutant that is reflected in the approximately 100 times lower association constant than found for the Q89L mutant. The association constant of Q89A and Q89L proteins (4 x 10(6) M(-1) and &gt;10(8) M(-1)) are 10- and 1,000-fold higher than that of the wild-type protein that forms conventional dimers clearly showing the energetic reasons for the flipped dimer formation.
+The line below this paragraph, {{ABSTRACT_PUBMED_11045631}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11045631 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11045631}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Bence-jones protein]]
 [[Category: Immunoglobulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:35:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 14:05:42 2008''