Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Truncated variants of gp120 bind CD4 with high affinity and suggest a minimum CD4 binding region.

The EMBO journal - 1 Feb 1992

Pollard S R, Rosa M D, Rosa J J, Wiley D C

Abstract excerpt

The envelope glycoprotein, gp120, of human immunodeficiency virus type 1 (HIV-1) binds the cellular protein CD4 with high affinity. By deletion we show that 62 N- and 20 C-terminal residues along with the V1, V2 and V3 variable regions of gp 120 are unnecessary for CD4 binding. A 287 residue variant (ENV59), missing those 197 amino acids, binds to CD4 with high affinity. A polyclonal antibody failed to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Cell Line
Share to Genetic Variation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Plasmids

Share to Polymerase Chain Reaction

Share to Protein Conformation

Share to Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 1537337
DOI: 10.1002/j.1460-2075.1992.tb05090.x
PMCID: PMC556490

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Truncated variants of gp120 bind CD4 with high affinity and suggest a minimum CD4 binding region.PMID 1537337Read ↗

The N-terminal region of the human immunodeficiency virus envelope glycoprotein gp120 contains potential binding sites for CD4.Semantic proximity Read ↗

Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding.Semantic proximity Read ↗

A region in domain 1 of CD4 distinct from the primary gp120 binding site is involved in HIV infection and virus-mediated fusion.Semantic proximity Read ↗

The genetic analysis of the HIV envelope binding domain on CD4.Semantic proximity Read ↗

A Recombinant Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex Stabilized by an Intermolecular Disulfide Bond between the gp120 and gp41 Subunits Is an Antigenic Mimic of the Trimeric Virion-Associated StructureSemantic proximity Read ↗

Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions.Semantic proximity Read ↗

Inhibition of human immunodeficiency virus (HIV-1) infectivity by expression of poorly or broadly neutralizing antibodies against Env in virus-producing cellsSemantic proximity Read ↗

Mutational Analysis of the Active Site and Antibody Epitopes of the Complement-inhibitory Glycoprotein, CD59Semantic proximity Read ↗

Contribution of charged amino acids in the CDR2 region of CD4 to HIV-1 gp120 binding.Semantic proximity Read ↗

Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion eventsSemantic proximity Read ↗

Use of a gp120 Binding Assay To Dissect the Requirements and Kinetics of Human Immunodeficiency Virus Fusion EventsSemantic proximity Read ↗

Recombinant CD4-selected human immunodeficiency virus type 1 variants with reduced gp120 affinity for CD4 and increased cell fusion capacity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.