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- PDB-2v5r: Structural basis for Dscam isoform specificity -

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Basic information

Entry
Database: PDB / ID: 2v5r
TitleStructural basis for Dscam isoform specificity
ComponentsDSCAM
KeywordsCELL ADHESION / DOWN SYNDROME CELL ADHESION MOLECULE DSCAM NEUROBIOLOGY SPL IMMUNOGLOBULIN DOMAIN / MEMBRANE / DEVELOPMENTAL PROTEIN
Function / homology
Function and homology information


detection of molecule of bacterial origin / mushroom body development / central nervous system morphogenesis / detection of mechanical stimulus involved in sensory perception of touch / dendrite self-avoidance / ventral cord development / axon extension involved in axon guidance / axon guidance receptor activity / peripheral nervous system development / axonal fasciculation ...detection of molecule of bacterial origin / mushroom body development / central nervous system morphogenesis / detection of mechanical stimulus involved in sensory perception of touch / dendrite self-avoidance / ventral cord development / axon extension involved in axon guidance / axon guidance receptor activity / peripheral nervous system development / axonal fasciculation / regulation of dendrite morphogenesis / neuron development / regulation of axonogenesis / phagocytosis / antigen binding / axon guidance / cell adhesion / neuron projection / axon / neuronal cell body / dendrite / integral component of plasma membrane / protein homodimerization activity / identical protein binding
Immunoglobulin subtype 2 / Immunoglobulin-like domain superfamily / Fibronectin type III / Immunoglobulin-like domain / Immunoglobulin I-set / Immunoglobulin-like fold / Down syndrome cell adhesion molecule, C-terminal / Immunoglobulin subtype / Fibronectin type III superfamily / Immunoglobulin I-set domain ...Immunoglobulin subtype 2 / Immunoglobulin-like domain superfamily / Fibronectin type III / Immunoglobulin-like domain / Immunoglobulin I-set / Immunoglobulin-like fold / Down syndrome cell adhesion molecule, C-terminal / Immunoglobulin subtype / Fibronectin type III superfamily / Immunoglobulin I-set domain / Basigin-like / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Down syndrome cell adhesion molecule 1, isoform BE / Dscam
Biological speciesDROSOPHILA MELANOGASTER (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsMeijers, R. / Puettmann-Holgado, R. / Skiniotis, G. / Liu, J.-H. / Walz, T. / Schmucker, D. / Wang, J.-H.
CitationJournal: Nature / Year: 2007
Title: Structural Basis of Dscam Isoform Specificity
Authors: Meijers, R. / Puettmann-Holgado, R. / Skiniotis, G. / Liu, J.-H. / Walz, T. / Wang, J.-H. / Schmucker, D.
Validation Report
SummaryFull reportAbout validation report
History
DepositionJul 9, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 11, 2007Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 23, 2019Group: Data collection / Database references / Other / Category: pdbx_database_status / struct_ref_seq_dif
Item: _pdbx_database_status.status_code_sf / _struct_ref_seq_dif.details
Revision 1.4Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DSCAM
B: DSCAM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)88,90612
Polymers86,9522
Non-polymers1,95410
Water0
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area690 Å2
ΔGint-7.6 kcal/mol
Surface area49080 Å2
MethodPQS
Unit cell
γ
α
β
Length a, b, c (Å)277.781, 70.548, 72.771
Angle α, β, γ (deg.)90.00, 105.13, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.863, -0.001, 0.506), (-1, -0.001), (0.506, -0.863)
Vector: -19.04812, -46.12549, 70.22813)
DetailsTHE DIMERIC STATE DESCRIBED IN REMARK 350 BELOW HASHAS BEEN EXPERIMENTALLY VALIDATED USIING BEAD AGGREGATIONASSAYS.

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Components

#1: Protein DSCAM / / DOWN SYNDROME CELL ADHESION MOLECULE DSCAM


Mass: 43476.008 Da / Num. of mol.: 2
Fragment: N-TERMINAL FOUR DOMAINS (D1, D2, D3 AND D4), RESIDUES 36-423
Source method: isolated from a genetically manipulated source
Details: ISOFORM 4.9/6.9 / Source: (gene. exp.) DROSOPHILA MELANOGASTER (fruit fly) / Organ: BRAIN / Variant: SPLICING VARIANT 4.9/6.9 / Plasmid: BACNBLUE / Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / References: UniProt: Q9NBA1, UniProt: Q0E9K4*PLUS
#2: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
Sequence detailsTHE CONFLICTS GIVEN IN THE SEQADV RECORDS BELOW ARE AS A RESULT OF A SPLICE VARIANT FORM OF THE ...THE CONFLICTS GIVEN IN THE SEQADV RECORDS BELOW ARE AS A RESULT OF A SPLICE VARIANT FORM OF THE PROTEIN WHERE EXON 4 COVERING RESIDUES 102 TO 156 CONSISTS OF ISOFORM 9 AND EXON 6 COVERING RESIDUES 205 TO 245 CONSISTS OF ISOFORM 9.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.9 Å3/Da / Density % sol: 69 % / Description: NONE
Crystal growDetails: 10 % PEG 8000, 1MM SPERMIDINE, 0.1 M TRISHCL PH 8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.979
DetectorType: ADSC CCD / Detector: CCD / Date: Jul 9, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 3→20 Å / Num. obs: 53580 / % possible obs: 86 % / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 10.9
Reflection shellResolution: 3→3.2 Å / Rmerge(I) obs: 0.23 / Mean I/σ(I) obs: 1.9 / % possible all: 55.5

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Processing

Software
NameClassification
PHENIXrefinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2V5M
Resolution: 3→20 Å
Details: B GROUP REFINEMENT NCS REFINEMENT DOMAIN D4 (RESIDUES 309-391) IS LESS WELL DEFINED
RfactorNum. reflection% reflection
Rfree0.303 -5 %
Rwork0.271 --
Obs-22250 86 %
Refinement stepCycle: LAST / Resolution: 3→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6108 0 124 0 6232

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