Acta Crystallogr D Struct Biol October 2020 PMID 33021501

The crystal structure of the tetrameric human vasohibin-1-SVBP complex reveals a variable arm region within the structural core.

Akihito Ikeda, Seia Urata, Tadashi Ando, Yasuhiro Suzuki, Yasufumi Sato, Tatsuya Nishino

Mentions

4
Peak: 2 in Apr 2021
across 2 sources since Sep 2020

Extended reach

6,010
potential audience

Total likes

0

Video views

65

Mentions per month

Sep 2020 – Apr 2021

Where it's discussed

  • X / Twitter2 posts
  • YouTube2 videos

AI synopsis

What people are saying

The group's discussions highlight key aspects like the discovery of a variable arm region in the structure, with phrases such as 'reveals a variable arm region' and references to structural insights, showing appreciation for the detailed findings. The tone is neutral and informative, indicating an overall acknowledgment of the research's scientific value without overly enthusiastic or dismissive sentiments.

AgreementModerate agreement

The posts acknowledge the significance of the structural findings, suggesting a general support or recognition of its importance in the field.

InterestModerate interest

The discussions reflect moderate curiosity, primarily focusing on the structural details and their implications.

EngagementNeutral engagement

Compared to deeper scientific discussions, most posts are brief and mainly share the publication without extensive analysis.

ImpactModerate impact

While the structure appears to be noteworthy for specialists, the overall perceived impact on broader biomedical fields seems modest.

Abstract in brief

  • Vasohibins play a crucial role in regulating processes like angiogenesis, tumor growth, and neuronal differentiation through their interaction with the small vasohibin-binding protein (SVBP).
  • Recent studies, including crystal structure determinations, have revealed insights into the complex's formation and function, but the regulatory mechanisms remain unclear.
  • This research specifically highlights the discovery of a novel domain-swapped heterotetramer structure that may influence enzyme activity due to the stabilization provided by conserved residues and differences in molecular dynamics compared to simpler structures.

Top posts

Most liked on X and Bluesky
Structural Biology
@ActaCrystD · X

Ikeda et al.: The crystal structure of the tetrameric human vasohibin-1–SVBP complex reveals a variable arm region within the structural core #ProteinComplexes @TUS_PR ... #IUCr https://t.co/9WQ0yNSFB1

Sep 16, 2020 · 3,023 followers View post →
African Synchrotron
@AfSynchrotron · X

The crystal structure of the tetrameric human vasohibin-1–SVBP complex reveals a variable arm region within the structural core https://t.co/tJojql3IYS via @ActaCrystD https://t.co/41OvQrjNIo

Oct 1, 2020 · 2,923 followers View post →

All mentions

African Synchrotron
@AfSynchrotron · X

The crystal structure of the tetrameric human vasohibin-1–SVBP complex reveals a variable arm region within the structural core https://t.co/tJojql3IYS via @ActaCrystD https://t.co/41OvQrjNIo

Oct 1, 2020 · 2,923 followers View post →
Structural Biology
@ActaCrystD · X

Ikeda et al.: The crystal structure of the tetrameric human vasohibin-1–SVBP complex reveals a variable arm region within the structural core #ProteinComplexes @TUS_PR ... #IUCr https://t.co/9WQ0yNSFB1

Sep 16, 2020 · 3,023 followers View post →