Evidence map›Paper›PMID 19368894›Full record

ArticleStructure (London, England : 1993)2009

The crystal structure of cobra venom factor, a cofactor for C3- and C5-convertase CVFBb.

Vengadesan Krishnan, Karthe Ponnuraj, Yuanyuan Xu, Kevin Macon, John E Volanakis, Sthanam V L Narayana

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 35 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Vengadesan KrishnanUniversity of Alabama at Birmingham, Birmingham, AL 35294, USA.
Karthe Ponnuraj
Yuanyuan Xu
Kevin Macon
John E Volanakis
Sthanam V L Narayana
University of Alabama at Birmingham · USUniversity of Madras · IN

Funding

Mechanism of Cell Surface Assembly Catalyzed by SortasesR01AI073521 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI STHANAM, NARAYANA VL · 2008 to 2012
$1.8M
NIAID NIH HHS AI1064815NIAID NIH HHS R01 AI073521
6 · The paper itself

Abstract

Cobra venom factor (CVF) is a functional analog of human complement component C3b, the active fragment of C3. Similar to C3b, in human and mammalian serum, CVF binds factor B, which is then cleaved by factor D, giving rise to the CVFBb complex that targets the same scissile bond in C3 as the authentic complement convertases C4bC2a and C3bBb. Unlike the latter, CVFBb is a stable complex and an efficient C5 convertase. We solved the crystal structure of CVF, isolated from Naja naja kouthia venom, at 2.6 A resolution. The CVF crystal structure, an intermediate between C3b and C3c, lacks the TED domain and has the CUB domain in an identical position to that seen in C3b. The similarly positioned CUB and slightly displaced C345c domains of CVF could play a vital role in the formation of C3 convertases by providing important primary binding sites for factor B.

Indexed as

AnimalsBinding SitesComplement C3bComplement C3-C5 ConvertasesComplement C3 Convertase, Alternative PathwayCrystallography, X-RayElapid VenomsModels, ChemicalModels, MolecularProtein BindingProtein Structure, SecondaryProtein Structure, Tertiarycobra venom factorComplement C3bComplement C3-C5 ConvertasesComplement C3 Convertase, Alternative PathwayElapid Venoms

Identifiers

PMID19368894
PMCPMC2671072
OpenAlexW2020429292

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.