Biomaterial Database

Homomeric interactions between transmembrane proteins of Moloney murine leukemia virus. 1996

X Li, and B McDermott, and B Yuan, and S P Goff

Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA.

We have studied homomeric interactions between transmembrane proteins (TM) of the Moloney murine leukemia virus envelope using the Saccharomyces cerevisiae two-hybrid system. TM interacts strongly with itself but not with various control proteins. Deletional and mutational analyses indicated that the putative leucine zipper motif in the extracellular domain of TM is essential and sufficient to mediate the binding. The first three repeats of the leucine zipper-like motif are the most important in mediating the interaction. The TM-TM interaction detected in this system may play a role in several stages of viral replication.

UI	MeSH Term	Description	Entries
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008979	Moloney murine leukemia virus	A strain of Murine leukemia virus (LEUKEMIA VIRUS, MURINE) arising during the propagation of S37 mouse sarcoma, and causing lymphoid leukemia in mice. It also infects rats and newborn hamsters. It is apparently transmitted to embryos in utero and to newborns through mother's milk.	Moloney Leukemia Virus,Leukemia Virus, Moloney,Virus, Moloney Leukemia
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D014759	Viral Envelope Proteins	Integral membrane proteins that are incorporated into the VIRAL ENVELOPE. They are glycosylated during VIRAL ASSEMBLY.	Envelope Proteins, Viral,Viral Envelope Glycoproteins,Viral Envelope Protein,Virus Envelope Protein,Virus Peplomer Proteins,Bovine Leukemia Virus Glycoprotein gp51,Hepatitis Virus (MHV) Glycoprotein E2,LaCrosse Virus Envelope Glycoprotein G1,Simian Sarcoma Virus Glycoprotein 70,Viral Envelope Glycoprotein gPr90 (Murine Leukemia Virus),Viral Envelope Glycoprotein gp55 (Friend Virus),Viral Envelope Proteins E1,Viral Envelope Proteins E2,Viral Envelope Proteins gp52,Viral Envelope Proteins gp70,Virus Envelope Proteins,Envelope Glycoproteins, Viral,Envelope Protein, Viral,Envelope Protein, Virus,Envelope Proteins, Virus,Glycoproteins, Viral Envelope,Peplomer Proteins, Virus,Protein, Viral Envelope,Protein, Virus Envelope,Proteins, Viral Envelope,Proteins, Virus Envelope,Proteins, Virus Peplomer
D015682	Retroviridae Proteins, Oncogenic	Retroviral proteins that have the ability to transform cells. They can induce sarcomas, leukemias, lymphomas, and mammary carcinomas. Not all retroviral proteins are oncogenic.	Oncogenic Retroviridae Proteins,Proteins, Oncogenic Retroviridae
D016350	Leucine Zippers	DNA-binding motifs formed from two alpha-helixes which intertwine for about eight turns into a coiled coil and then bifurcate to form Y shaped structures. Leucines occurring in heptad repeats end up on the same sides of the helixes and are adjacent to each other in the stem of the Y (the "zipper" region). The DNA-binding residues are located in the bifurcated region of the Y.	Leucine Zipper,Zipper, Leucine,Zippers, Leucine