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.


4lve

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4lve.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:4lve.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4lve| PDB=4lve | SCENE= }}
{{STRUCTURE_4lve| PDB=4lve | SCENE= }}
-
'''LEN K30T MUTANT: A DOMAIN FLIP AS A RESULT OF A SINGLE AMINO ACID SUBSTITUTION'''
+
===LEN K30T MUTANT: A DOMAIN FLIP AS A RESULT OF A SINGLE AMINO ACID SUBSTITUTION===
-
==Overview==
+
<!--
-
BACKGROUND: The self-assembly properties of beta domains are important features of diverse classes of proteins that include cell-adhesion molecules, surface receptors and the immunoglobulin superfamily. Immunoglobulin light-chain variable domains are well suited to the study of structural factors that determine dimerization, including how residues at the interface influence the preferred dimer arrangement. RESULTS: Single-site mutants of light-chain variable domain Len, designated LenQ38E and LenK30T, formed 'flipped' dimers in which one domain was rotated by about 180 degrees compared with the native protein. The dimer in the native protein is similar to that found between variable domains in Fab immunoglobulin fragments. When compared to the native dimer, more surface area is buried, and more hydrogen bonds and salt bridges are formed between the monomers in the flipped conformation. CONCLUSIONS: Immunoglobulin light-chain variable domains can form a minimum of two distinct quaternary structures. Single-site mutations resulting from changes of one base, such as the exchange of Gln38 to Glu or Lys30 to Thr, change the 'conventional' dimer of protein Len to a flipped arrangement. Native Len is not found in the flipped-domain dimer conformation because it would have excess positive electrostatic potential at the dimer interface that is not compensated by other forces. Excess negative or positive electrostatic potential at the dimer interface can have a determining effect on the mode of dimerization.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9739086}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9739086 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9739086}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Kappa-iv]]
[[Category: Kappa-iv]]
[[Category: Light chain dimer]]
[[Category: Light chain dimer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:26:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:43:07 2008''

Revision as of 10:43, 3 July 2008

Image:4lve.png

Template:STRUCTURE 4lve

LEN K30T MUTANT: A DOMAIN FLIP AS A RESULT OF A SINGLE AMINO ACID SUBSTITUTION

Template:ABSTRACT PUBMED 9739086

About this Structure

4LVE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A domain flip as a result of a single amino-acid substitution., Pokkuluri PR, Huang DB, Raffen R, Cai X, Johnson G, Stevens PW, Stevens FJ, Schiffer M, Structure. 1998 Aug 15;6(8):1067-73. PMID:9739086

Page seeded by OCA on Thu Jul 3 13:43:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lve"
Personal tools