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Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains.

Identifieur interne : 003D00 ( Main/Exploration ); précédent : 003C99; suivant : 003D01

Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains.

Auteurs : Karen H Nel [Allemagne] ; Thomas Stangler ; Matthias Stoldt ; Dieter Willbold

Source :

RBID : pubmed:16328780

Descripteurs français

English descriptors

Abstract

The SARS related Coronavirus genome contains a variety of novel accessory genes. One of these, called ORF7a or ORF8, code for a protein, known as 7a, U122 or X4. We set out to determine the three-dimensional structure of the soluble ectodomain of this type-I transmembrane protein by nuclear magnetic resonance spectroscopy. The fold of the protein is the first member of a further variation of the immunoglobulin like beta-sandwich fold. Because X4 does not reveal significant sequence homologies to proteins in the data bases, we carried out a structure based similarity search for proteins with known function. High structural similarity to Dl domains of ICAM-1 and ICAM-2, and common features in amino acid sequence between X4 and ICAM-1, suggest X4 to possess binding activity for the alpha(L) integrin I domain of LFA-1. Further, based on this structure based prediction, potential functions of X4 in virus replication and pathogenesis are discussed.

DOI: 10.1007/s11373-005-9043-9
PubMed: 16328780


Affiliations:


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Le document en format XML

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<term>Antigens, CD (chemistry)</term>
<term>Cell Adhesion Molecules (chemistry)</term>
<term>Cloning, Molecular</term>
<term>Humans</term>
<term>Immunoglobulins (chemistry)</term>
<term>Integrins (chemistry)</term>
<term>Intercellular Adhesion Molecule-1 (chemistry)</term>
<term>Interleukin-1 (chemistry)</term>
<term>Lymphocyte Function-Associated Antigen-1 (chemistry)</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Open Reading Frames</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>SARS Virus (chemistry)</term>
<term>Viral Matrix Proteins (chemistry)</term>
<term>Viral Proteins (chemistry)</term>
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<term>Antigène-1 associé à la fonction du lymphocyte ()</term>
<term>Antigènes CD ()</term>
<term>Cadres ouverts de lecture</term>
<term>Clonage moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Immunoglobulines ()</term>
<term>Interleukine-1 ()</term>
<term>Intégrines ()</term>
<term>Modèles moléculaires</term>
<term>Molécule-1 d'adhérence intercellulaire ()</term>
<term>Molécules d'adhérence cellulaire ()</term>
<term>Protéines de la matrice virale ()</term>
<term>Protéines virales ()</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS ()</term>
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<term>Antigens, CD</term>
<term>Cell Adhesion Molecules</term>
<term>Immunoglobulins</term>
<term>Integrins</term>
<term>Intercellular Adhesion Molecule-1</term>
<term>Interleukin-1</term>
<term>Lymphocyte Function-Associated Antigen-1</term>
<term>Viral Matrix Proteins</term>
<term>Viral Proteins</term>
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<term>SARS Virus</term>
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<term>Humans</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Open Reading Frames</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
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<term>Antigène-1 associé à la fonction du lymphocyte</term>
<term>Antigènes CD</term>
<term>Cadres ouverts de lecture</term>
<term>Clonage moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Immunoglobulines</term>
<term>Interleukine-1</term>
<term>Intégrines</term>
<term>Modèles moléculaires</term>
<term>Molécule-1 d'adhérence intercellulaire</term>
<term>Molécules d'adhérence cellulaire</term>
<term>Protéines de la matrice virale</term>
<term>Protéines virales</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
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<div type="abstract" xml:lang="en">The SARS related Coronavirus genome contains a variety of novel accessory genes. One of these, called ORF7a or ORF8, code for a protein, known as 7a, U122 or X4. We set out to determine the three-dimensional structure of the soluble ectodomain of this type-I transmembrane protein by nuclear magnetic resonance spectroscopy. The fold of the protein is the first member of a further variation of the immunoglobulin like beta-sandwich fold. Because X4 does not reveal significant sequence homologies to proteins in the data bases, we carried out a structure based similarity search for proteins with known function. High structural similarity to Dl domains of ICAM-1 and ICAM-2, and common features in amino acid sequence between X4 and ICAM-1, suggest X4 to possess binding activity for the alpha(L) integrin I domain of LFA-1. Further, based on this structure based prediction, potential functions of X4 in virus replication and pathogenesis are discussed.</div>
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