Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit

Wilma Puzon-McLaughlin, Yoshikazu Takada

Research output: Contribution to journalArticle

78 Citations (Scopus)

Abstract

Several integrin α subunits have an inserted sequence of about 200 residues (the I or A domain) that is critical for ligand interactions. The presence of an I domain-like structure within the integrin β subunit has been proposed based on the similarity of the hydropathy profiles and the homology of sequences between the α and β subunits. This study was designed to determine whether the region of the β1 subunit that includes residues 101335 has the characteristics of an I domain. We found novel critical residues for ligand binding (Ser-132, Asn-224, Asp-226, Glu-229, Asp-233, Asp-267, and Asp-295, in addition to the previously reported Asp-130) using site-directed mutagenesis. The critical residues for ligand binding are located in several of loop structures of the region (or in a potential loop between an α helix and a β strand), which have been predicted using multiple secondary structure prediction methods. The data suggest that the β subunit has multiple disrupted critical oxygenated residues for ligand binding similar to those found in the α I domain.

Original languageEnglish (US)
Pages (from-to)20438-20443
Number of pages6
JournalJournal of Biological Chemistry
Volume271
Issue number34
DOIs
StatePublished - 1996
Externally publishedYes

Fingerprint

Integrins
Ligands
Mutagenesis
Sequence Homology
Site-Directed Mutagenesis

ASJC Scopus subject areas

  • Biochemistry

Cite this

Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit. / Puzon-McLaughlin, Wilma; Takada, Yoshikazu.

In: Journal of Biological Chemistry, Vol. 271, No. 34, 1996, p. 20438-20443.

Research output: Contribution to journalArticle

@article{c8e3883ee0014868bfd7a7307e5ffa0e,
title = "Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit",
abstract = "Several integrin α subunits have an inserted sequence of about 200 residues (the I or A domain) that is critical for ligand interactions. The presence of an I domain-like structure within the integrin β subunit has been proposed based on the similarity of the hydropathy profiles and the homology of sequences between the α and β subunits. This study was designed to determine whether the region of the β1 subunit that includes residues 101335 has the characteristics of an I domain. We found novel critical residues for ligand binding (Ser-132, Asn-224, Asp-226, Glu-229, Asp-233, Asp-267, and Asp-295, in addition to the previously reported Asp-130) using site-directed mutagenesis. The critical residues for ligand binding are located in several of loop structures of the region (or in a potential loop between an α helix and a β strand), which have been predicted using multiple secondary structure prediction methods. The data suggest that the β subunit has multiple disrupted critical oxygenated residues for ligand binding similar to those found in the α I domain.",
author = "Wilma Puzon-McLaughlin and Yoshikazu Takada",
year = "1996",
doi = "10.1074/jbc.271.34.20438",
language = "English (US)",
volume = "271",
pages = "20438--20443",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "34",

}

TY - JOUR

T1 - Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit

AU - Puzon-McLaughlin, Wilma

AU - Takada, Yoshikazu

PY - 1996

Y1 - 1996

N2 - Several integrin α subunits have an inserted sequence of about 200 residues (the I or A domain) that is critical for ligand interactions. The presence of an I domain-like structure within the integrin β subunit has been proposed based on the similarity of the hydropathy profiles and the homology of sequences between the α and β subunits. This study was designed to determine whether the region of the β1 subunit that includes residues 101335 has the characteristics of an I domain. We found novel critical residues for ligand binding (Ser-132, Asn-224, Asp-226, Glu-229, Asp-233, Asp-267, and Asp-295, in addition to the previously reported Asp-130) using site-directed mutagenesis. The critical residues for ligand binding are located in several of loop structures of the region (or in a potential loop between an α helix and a β strand), which have been predicted using multiple secondary structure prediction methods. The data suggest that the β subunit has multiple disrupted critical oxygenated residues for ligand binding similar to those found in the α I domain.

AB - Several integrin α subunits have an inserted sequence of about 200 residues (the I or A domain) that is critical for ligand interactions. The presence of an I domain-like structure within the integrin β subunit has been proposed based on the similarity of the hydropathy profiles and the homology of sequences between the α and β subunits. This study was designed to determine whether the region of the β1 subunit that includes residues 101335 has the characteristics of an I domain. We found novel critical residues for ligand binding (Ser-132, Asn-224, Asp-226, Glu-229, Asp-233, Asp-267, and Asp-295, in addition to the previously reported Asp-130) using site-directed mutagenesis. The critical residues for ligand binding are located in several of loop structures of the region (or in a potential loop between an α helix and a β strand), which have been predicted using multiple secondary structure prediction methods. The data suggest that the β subunit has multiple disrupted critical oxygenated residues for ligand binding similar to those found in the α I domain.

UR - http://www.scopus.com/inward/record.url?scp=0029786408&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029786408&partnerID=8YFLogxK

U2 - 10.1074/jbc.271.34.20438

DO - 10.1074/jbc.271.34.20438

M3 - Article

C2 - 8702782

AN - SCOPUS:0029786408

VL - 271

SP - 20438

EP - 20443

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 34

ER -