We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2p26

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2p26.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2p26.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2p26| PDB=2p26 | SCENE= }}
{{STRUCTURE_2p26| PDB=2p26 | SCENE= }}
-
'''Structure of the PHE2 and PHE3 fragments of the integrin beta2 subunit'''
+
===Structure of the PHE2 and PHE3 fragments of the integrin beta2 subunit===
-
==Overview==
+
<!--
-
Integrins mediate cell adhesion in response to activation signals that trigger conformational changes within their ectodomain. It is thought that a compact bent conformation of the molecule represents its physiological low affinity state and extended conformations its active state. We have determined the structure of two integrin fragments of the beta2 subunit. The first structure, consisting of the plexin-semaphorin-integrin domain, hybrid, integrin-epidermal growth factor 1 (I-EGF1), and I-EGF2 domains (PHE2), showed an L-shaped conformation with the bend located between the I-EGF1 and I-EGF2 domains. The second structure, which includes, in addition, the I-EGF3 domain, showed an extended conformation. The major reorientation of I-EGF2 with respect to the other domains in the two structures is accompanied by a change of torsion angle of the disulfide bond between Cys(461)-Cys(492) by 180 degrees and the conversion of a short alpha-helix (residues Ser(468)-Cys(475)) into a flexible coil. Based on the PHE2 structure, we introduced a disulfide bond between the plexin-semaphorin-integrin domain and I-EGF2 domains in the beta2 subunit. The resultant alphaLbeta2 integrin (leukocyte function-associated antigen-1) variant was locked in a bent state and could not be detected with the monoclonal antibody KIM127 in Mg(2+)/EGTA. However, it retained the binding activity to ICAM-1. These results provide a structural hypothesis for our understanding of the transition between the resting and active states of leukocyte function-associated antigen-1.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17673459}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17673459 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17673459}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Integrin beta2 subunit]]
[[Category: Integrin beta2 subunit]]
[[Category: Psi domain]]
[[Category: Psi domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:16:30 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:38:54 2008''

Revision as of 15:38, 27 July 2008

Image:2p26.png

Template:STRUCTURE 2p26

Structure of the PHE2 and PHE3 fragments of the integrin beta2 subunit

Template:ABSTRACT PUBMED 17673459

About this Structure

2P26 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A structural hypothesis for the transition between bent and extended conformations of the leukocyte beta2 integrins., Shi M, Foo SY, Tan SM, Mitchell EP, Law SK, Lescar J, J Biol Chem. 2007 Oct 12;282(41):30198-206. Epub 2007 Aug 1. PMID:17673459

Page seeded by OCA on Sun Jul 27 18:38:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p26"
Personal tools