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.


1ic1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ic1.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ic1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ic1| PDB=1ic1 | SCENE= }}
{{STRUCTURE_1ic1| PDB=1ic1 | SCENE= }}
-
'''THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1'''
+
===THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1===
-
==Overview==
+
<!--
-
The 3.0-A structure of a 190-residue fragment of intercellular adhesion molecule-1 (ICAM-1, CD54) reveals two tandem Ig-superfamily (IgSF) domains. Each of two independent molecules dimerizes identically with a symmetry-related molecule over a hydrophobic interface on the BED sheet of domain 1, in agreement with dimerization of ICAM-1 on the cell surface. The residues that bind to the integrin LFA-1 are well oriented for bivalent binding in the dimer, with the critical Glu-34 residues pointing away from each other on the periphery. Residues that bind to rhinovirus are in the flexible BC and FG loops at the tip of domain 1, and these and the upper half of domain 1 are well exposed in the dimer for docking to virus. By contrast, a residue important for binding to Plasmodium falciparum-infected erythrocytes is in the dimer interface. The presence of A' strands in both domains 1 and 2, conserved hydrogen bonds at domain junctions, and elaborate hydrogen bond networks around the key integrin binding residues in domain 1 make these domains suited to resist tensile forces during adhesive interactions. A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9539702}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9539702 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9539702}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Icam-1]]
[[Category: Icam-1]]
[[Category: Immunoglobulin fold]]
[[Category: Immunoglobulin fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:49:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:44:26 2008''

Revision as of 07:44, 1 July 2008

Image:1ic1.png

Template:STRUCTURE 1ic1

THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1

Template:ABSTRACT PUBMED 9539702

About this Structure

1IC1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1., Casasnovas JM, Stehle T, Liu JH, Wang JH, Springer TA, Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4134-9. PMID:9539702

Page seeded by OCA on Tue Jul 1 10:44:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ic1"
Personal tools