Evidence map›Paper›PMID 26198801›Full record

ArticleAndrology2015

Sperm Lysozyme-Like Protein 1 (SLLP1), an intra-acrosomal oolemmal-binding sperm protein, reveals filamentous organization in protein crystal form.

H Zheng, A Mandal, I A Shumilin, M D Chordia, S Panneerdoss, J C Herr, W Minor

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Andrology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 19% 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

5 citing papers in PubMed, 13 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

7 authors at 1 institution in 1 country.

H ZhengDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.
A MandalDepartment of Cell Biology, Center for Research in Contraceptive and Reproductive Health, University of Virginia, Charlottesville, VA, USA.
I A ShumilinDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.
M D ChordiaDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.
S PanneerdossDepartment of Cell Biology, Center for Research in Contraceptive and Reproductive Health, University of Virginia, Charlottesville, VA, USA.
J C HerrDepartment of Cell Biology, Center for Research in Contraceptive and Reproductive Health, University of Virginia, Charlottesville, VA, USA.
W MinorDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.
University of Virginia · US

Funding

THE MIDWEST CENTER FOR STRUCTURAL GENOMICSP50GM062414 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ JOACHIMIAK · 2000 to 2004
$33.2M
X-RAY CRYSTALLOGRAPHY OF MACROMOLECULESR01GM053163 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MINOR, WLADEK, OTWINOWSKI, ZBYSZEK · 1996 to 2014
$6.3M
Structural Targeting Testis Specific Kinases (TSSK) 1 & 2 for Male ContraceptionU01HD060491 · NICHD · UNIVERSITY OF VIRGINIA · PI HERR, JOHN C · 2009 to 2013
$1.3M
NICHD NIH HHS D43TW/HD00654NICHD NIH HHS U01 HD060491NICHD NIH HHS U01HD60491NIGMS NIH HHS GM53163NIGMS NIH HHS GM62414NIGMS NIH HHS P50 GM062414NIGMS NIH HHS R01 GM053163
6 · The paper itself

Abstract

Sperm lysozyme-like protein 1 (SLLP1) is one of the lysozyme-like proteins predominantly expressed in mammalian testes that lacks bacteriolytic activity, localizes in the sperm acrosome, and exhibits high affinity for an oolemmal receptor, SAS1B. The crystal structure of mouse SLLP1 (mSLLP1) was determined at 2.15 Å resolution. mSLLP1 monomer adopts a structural fold similar to that of chicken/mouse lysozymes retaining all four canonical disulfide bonds. mSLLP1 is distinct from c-lysozyme by substituting two essential catalytic residues (E35T/D52N), exhibiting different surface charge distribution, and by forming helical filaments approximately 75 Å in diameter with a 25 Å central pore comprised of six monomers per helix turn repeating every 33 Å. Cross-species alignment of all reported SLLP1 sequences revealed a set of invariant surface regions comprising a characteristic fingerprint uniquely identifying SLLP1 from other c-lysozyme family members. The fingerprint surface regions reside around the lips of the putative glycan-binding groove including three polar residues (Y33/E46/H113). A flexible salt bridge (E46-R61) was observed covering the glycan-binding groove. The conservation of these regions may be linked to their involvement in oolemmal protein binding. Interaction between SLLP1 monomer and its oolemmal receptor SAS1B was modeled using protein-protein docking algorithms, utilizing the SLLP1 fingerprint regions along with the SAS1B conserved surface regions. This computational model revealed complementarity between the conserved SLLP1/SAS1B interacting surfaces supporting the experimentally observed SLLP1/SAS1B interaction involved in fertilization.

Indexed as

AnimalsCrystallizationEscherichia coliFemaleIsoantigensMiceMolecular ConformationRecombinant ProteinsSeminal Plasma ProteinsIsoantigensRecombinant ProteinsSeminal Plasma ProteinsSLLP1 protein, mousecrystal structurefertilizationprotein-protein interactionrefoldingSAS1BSLLP1

Identifiers

PMID26198801
PMCPMC5040164
OpenAlexW2108031923

What OpenQuestion holds

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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.