Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin

Aidong Qu, Daniel J. Leahy

Research output: Contribution to journalArticle

Abstract

We report the 1.8-Å crystal structure of the CD11a I-domain with bound manganese ion. The CD11a I-domain contains binding sites for intercellular adhesion molecules 1 and 3 and can exist in both low- and high-affinity states. The metal-bound form reported here is likely to represent a high-affinity state. The CD11a I-domain structure reveals a strained hydrophobic ridge adjacent to the bound metal ion that may serve as a ligand-binding surface and is likely to rearrange in the absence of bound metal ion. The CD11a I-domain is homologous to domains found in von Willebrand factor, and mapping of mutations found in types 2a and 2b von Willebrand disease onto this structure allows consideration of the molecular basis of these forms of the disease.

Original languageEnglish (US)
Pages (from-to)10277-10281
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number22
StatePublished - Oct 24 1995

Fingerprint

Lymphocyte Function-Associated Antigen-1
Type 2 von Willebrand Disease
Integrins
Metals
Ions
von Willebrand Factor
Intercellular Adhesion Molecule-1
Manganese
Binding Sites
Ligands
Mutation

Keywords

  • Cell-cell adhesion
  • Metal-binding site
  • Protein structure
  • Von Willebrand disease

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin. / Qu, Aidong; Leahy, Daniel J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, No. 22, 24.10.1995, p. 10277-10281.

Research output: Contribution to journalArticle

@article{d215ade3acc04147b45d2c9583ec67b7,
title = "Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin",
abstract = "We report the 1.8-{\AA} crystal structure of the CD11a I-domain with bound manganese ion. The CD11a I-domain contains binding sites for intercellular adhesion molecules 1 and 3 and can exist in both low- and high-affinity states. The metal-bound form reported here is likely to represent a high-affinity state. The CD11a I-domain structure reveals a strained hydrophobic ridge adjacent to the bound metal ion that may serve as a ligand-binding surface and is likely to rearrange in the absence of bound metal ion. The CD11a I-domain is homologous to domains found in von Willebrand factor, and mapping of mutations found in types 2a and 2b von Willebrand disease onto this structure allows consideration of the molecular basis of these forms of the disease.",
keywords = "Cell-cell adhesion, Metal-binding site, Protein structure, Von Willebrand disease",
author = "Aidong Qu and Leahy, {Daniel J.}",
year = "1995",
month = "10",
day = "24",
language = "English (US)",
volume = "92",
pages = "10277--10281",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "22",

}

TY - JOUR

T1 - Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin

AU - Qu, Aidong

AU - Leahy, Daniel J.

PY - 1995/10/24

Y1 - 1995/10/24

N2 - We report the 1.8-Å crystal structure of the CD11a I-domain with bound manganese ion. The CD11a I-domain contains binding sites for intercellular adhesion molecules 1 and 3 and can exist in both low- and high-affinity states. The metal-bound form reported here is likely to represent a high-affinity state. The CD11a I-domain structure reveals a strained hydrophobic ridge adjacent to the bound metal ion that may serve as a ligand-binding surface and is likely to rearrange in the absence of bound metal ion. The CD11a I-domain is homologous to domains found in von Willebrand factor, and mapping of mutations found in types 2a and 2b von Willebrand disease onto this structure allows consideration of the molecular basis of these forms of the disease.

AB - We report the 1.8-Å crystal structure of the CD11a I-domain with bound manganese ion. The CD11a I-domain contains binding sites for intercellular adhesion molecules 1 and 3 and can exist in both low- and high-affinity states. The metal-bound form reported here is likely to represent a high-affinity state. The CD11a I-domain structure reveals a strained hydrophobic ridge adjacent to the bound metal ion that may serve as a ligand-binding surface and is likely to rearrange in the absence of bound metal ion. The CD11a I-domain is homologous to domains found in von Willebrand factor, and mapping of mutations found in types 2a and 2b von Willebrand disease onto this structure allows consideration of the molecular basis of these forms of the disease.

KW - Cell-cell adhesion

KW - Metal-binding site

KW - Protein structure

KW - Von Willebrand disease

UR - http://www.scopus.com/inward/record.url?scp=0028822128&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028822128&partnerID=8YFLogxK

M3 - Article

C2 - 7479767

AN - SCOPUS:0028822128

VL - 92

SP - 10277

EP - 10281

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

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

SN - 0027-8424

IS - 22

ER -