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

Solution Structure of the Kaposi's Sarcoma-associated Herpesvirus K3 N-terminal Domain Reveals a Novel E2-binding C4HC3-type RING Domain

1 Dec 2004

Abstract excerpt

RING domains are found in a large number of eukaryotic proteins. Most function as E3 ubiquitin-protein ligases, catalyzing the terminal step in the ubiquitination process. Structurally, these domains have been characterized as binding two zinc ions in a stable cross-brace motif. The tumorigenic human gamma-herpesvirus Kaposi's sarcoma-associated herpesvirus encodes a ubiquitin-protein ligase termed K3, which...

Read the complete abstract on PubMed

Topics

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

Share to Cytomegalovirus and herpesvirus research
Share to Herpesvirus Infections and Treatments
Share to Viral-associated cancers and disorders

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15465811
DOI: 10.1074/jbc.m409662200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Solution Structure of the Kaposi's Sarcoma-associated Herpesvirus K3 N-terminal Domain Reveals a Novel E2-binding C4HC3-type RING DomainPMID 15465811Read ↗

c-MIR, a Human E3 Ubiquitin Ligase, Is a Functional Homolog of Herpesvirus Proteins MIR1 and MIR2 and Has Similar ActivitySemantic proximity Read ↗

Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade.Semantic proximity Read ↗

Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger‐mediated dimerizationSemantic proximity Read ↗

Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING.Semantic proximity Read ↗

Selective dimerization of a C2H2 zinc finger subfamily.Semantic proximity Read ↗

The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase familySemantic proximity Read ↗

Poxvirus K7 Protein Adopts a Bcl-2 Fold: Biochemical Mapping of Its Interactions with Human DEAD Box RNA Helicase DDX3Semantic proximity Read ↗

How kelch domain-containing protein 3 distinguishes between the C-end degron of herpesviral protein UL49.5 and its mutants - Insights from molecular dynamics.Semantic proximity Read ↗

Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains.Semantic proximity Read ↗

The DTX Protein Family: An Emerging Set of E3 Ubiquitin Ligases in CancerSemantic proximity Read ↗

KLHL9 acts as a KSHV vBcl-2-interacting host factor that supports lytic replicationSemantic proximity Read ↗

K15 Protein of Kaposi’s Sarcoma-Associated Herpesvirus Is Latently Expressed and Binds to HAX-1, a Protein with Antiapoptotic FunctionSemantic proximity Read ↗

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