A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1 (Q27749058)

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J H Liu

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J H Wang

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T A Springer

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

14 April 1998

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published in

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volume

95

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issue

8

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page(s)

4134-9

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Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains

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A Binding Interface on the I Domain of Lymphocyte Function-associated Antigen-1 (LFA-1) Required for Specific Interaction with Intercellular Adhesion Molecule 1 (ICAM-1)

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The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site

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Kinetics and thermodynamics of virus binding to receptor. Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance

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A soluble form of intercellular adhesion molecule-1 inhibits rhinovirus infection

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Plasmodium falciparum-infected erythrocytes bind ICAM-1 at a site distinct from LFA-1, Mac-1, and human rhinovirus

2 June 2018

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α4 Integrin Binding Interfaces on VCAM-1 and MAdCAM-1

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12 December 2020

Role of alpha L beta 2 integrin avidity in transendothelial chemotaxis of mononuclear cells

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12 December 2020

Specific versus non-specific contacts in protein crystals

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12 December 2020

Location of the domains of ICAM-1 by immunolabeling and single-molecule electron microscopy

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12 December 2020

The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. Correlation with binding to LFA-1

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12 December 2020

The neuronal glycoprotein telencephalin is a cellular ligand for the CD11a/CD18 leukocyte integrin

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12 December 2020

Identifiers

DOI

10.1073/PNAS.95.8.4134

1 reference

ADS bibcode

1998PNAS...95.4134C

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1 reference

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PubMed publication ID

9539702

1 reference