3RDV

Structure of the SLAIN2c-CLIPCG1 complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.180 
  • R-Value Observed: 0.184 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase

van der Vaart, B.Manatschal, C.Grigoriev, I.Olieric, V.Gouveia, S.M.Bjelic, S.Demmers, J.Vorobjev, I.Hoogenraad, C.C.Steinmetz, M.O.Akhmanova, A.

(2011) J Cell Biol 193: 1083-1099

  • DOI: https://doi.org/10.1083/jcb.201012179
  • Primary Citation of Related Structures:  
    3RDV

  • PubMed Abstract: 

    The ends of growing microtubules (MTs) accumulate a set of diverse factors known as MT plus end-tracking proteins (+TIPs), which control microtubule dynamics and organization. In this paper, we identify SLAIN2 as a key component of +TIP interaction networks. We showed that the C-terminal part of SLAIN2 bound to end-binding proteins (EBs), cytoplasmic linker proteins (CLIPs), and CLIP-associated proteins and characterized in detail the interaction of SLAIN2 with EB1 and CLIP-170. Furthermore, we found that the N-terminal part of SLAIN2 interacted with ch-TOG, the mammalian homologue of the MT polymerase XMAP215. Through its multiple interactions, SLAIN2 enhanced ch-TOG accumulation at MT plus ends and, as a consequence, strongly stimulated processive MT polymerization in interphase cells. Depletion or disruption of the SLAIN2-ch-TOG complex led to disorganization of the radial MT array. During mitosis, SLAIN2 became highly phosphorylated, and its interaction with EBs and ch-TOG was inhibited. Our study provides new insights into the molecular mechanisms underlying cell cycle-specific regulation of MT polymerization and the organization of the MT network.


  • Organizational Affiliation

    Department of Cell Biology, Erasmus Medical Center, 3000 CA Rotterdam, Netherlands.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CAP-Gly domain-containing linker protein 1
A, B, C, D
72Homo sapiensMutation(s): 0 
Gene Names: CLIP-170
UniProt & NIH Common Fund Data Resources
Find proteins for P30622 (Homo sapiens)
Explore P30622 
Go to UniProtKB:  P30622
PHAROS:  P30622
GTEx:  ENSG00000130779 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP30622
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
SLAIN motif-containing protein 2
E, F, G, H
8Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q9P270 (Homo sapiens)
Explore Q9P270 
Go to UniProtKB:  Q9P270
PHAROS:  Q9P270
GTEx:  ENSG00000109171 
Entity Groups  
UniProt GroupQ9P270
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.180 
  • R-Value Observed: 0.184 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.21α = 100.06
b = 45.74β = 105.76
c = 49.36γ = 108.39
Software Package:
Software NamePurpose
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
RemDAqdata collection
XDSdata reduction
BALBESphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-06-29
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-11-08
    Changes: Refinement description
  • Version 1.3: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description