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.


1zxq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zxq.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zxq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zxq| PDB=1zxq | SCENE= }}
{{STRUCTURE_1zxq| PDB=1zxq | SCENE= }}
-
'''THE CRYSTAL STRUCTURE OF ICAM-2'''
+
===THE CRYSTAL STRUCTURE OF ICAM-2===
-
==Overview==
+
<!--
-
Recognition by integrin proteins on the cell surface regulates the adhesive interactions between cells and their surroundings. The structure of the 'I' domain that is found in some but not all integrins, has been determined. However, the only integrin ligands for which structures are known, namely fibronectin and VCAM-1, are recognized by integrins that lack I domains. The intercellular adhesion molecules ICAM-1, 2 and 3 are, like VCAM-1, members of the immunoglobulin superfamily (IgSF), but they are recognized by an I domain-containing integrin, lymphocyte-function-associated antigen 1 (LFA-1, or CD11a/CD18). Here we present the crystal structure of the extracellular region of ICAM-2. The glutamic acid residue at position 37 is critical for LFA-1 binding and is proposed to coordinate the Mg2+ ion in the I domain; this Glu 37 is surrounded by a relatively flat recognition surface and lies in a beta-strand, whereas the critical aspartic acid residue in VCAM-1 and fibronectin lie in protruding loops. This finding suggests that there are differences in the architecture of recognition sites between integrins that contain or lack I domains. A bend between domains 1 and 2 of ICAM-2 and a tripod-like arrangement of N-linked glycans in the membrane-proximal region of domain 2 may be important for presenting the recognition surface to LFA-1. A model of ICAM-1 based on the ICAM-2 structure provides a framework for understanding its recognition by pathogens.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9153399}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9153399 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9153399}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Signal]]
[[Category: Signal]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:12:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:13:57 2008''

Revision as of 13:14, 27 July 2008

Template:STRUCTURE 1zxq

THE CRYSTAL STRUCTURE OF ICAM-2

Template:ABSTRACT PUBMED 9153399

About this Structure

1ZXQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface., Casasnovas JM, Springer TA, Liu JH, Harrison SC, Wang JH, Nature. 1997 May 15;387(6630):312-5. PMID:9153399

Page seeded by OCA on Sun Jul 27 16:13:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools