PDBsum entry 3lue

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protein Protein-protein interface(s) links
Structural protein PDB id
Protein chains
(+ 4 more) 374 a.a.
(+ 4 more) 109 a.a. *
* Residue conservation analysis
PDB id:
Name: Structural protein
Title: Model of alpha-actinin ch1 bound to f-actin
Structure: Actin, cytoplasmic 1. Chain: a, b, c, d, e, f, g, h, i, j. Synonym: beta-actin, actin, cytoplasmic 1, n-terminally pro engineered: yes. Alpha-actinin-3. Chain: k, m, l, o, n, q, p, s, r, t. Synonym: alpha-actinin skeletal muscle isoform 3, f-actin c linking protein. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: actb. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: actn3. Expression_system_taxid: 562
Authors: V.E.Galkin,A.Orlova,A.Salmazo,K.Djinovic-Carugo,E.H.Egelman
Key ref: V.E.Galkin et al. (2010). Opening of tandem calponin homology domains regulates their affinity for F-actin. Nat Struct Mol Biol, 17, 614-616. PubMed id: 20383143
17-Feb-10     Release date:   28-Apr-10    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P60709  (ACTB_HUMAN) -  Actin, cytoplasmic 1
375 a.a.
374 a.a.
Protein chains
Pfam   ArchSchema ?
Q08043  (ACTN3_HUMAN) -  Alpha-actinin-3
901 a.a.
109 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular space   17 terms 
  Biological process     Fc-gamma receptor signaling pathway involved in phagocytosis   17 terms 
  Biochemical function     RNA polymerase II core promoter proximal region sequence-specific DNA binding     12 terms  


Nat Struct Mol Biol 17:614-616 (2010)
PubMed id: 20383143  
Opening of tandem calponin homology domains regulates their affinity for F-actin.
V.E.Galkin, A.Orlova, A.Salmazo, K.Djinovic-Carugo, E.H.Egelman.
Many actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH domains of alpha-actinin to be in a compact, closed conformation, but the interpretations of complexes of such tandem CH domains with F-actin have been ambiguous. We show that the tandem CH domains of alpha-actinin bind F-actin in an open conformation, explaining mutations that cause human diseases and suggesting that the opening of these domains may be one of the main regulatory mechanisms for proteins with tandem CH domains.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20644981 R.Umemoto, N.Nishida, S.Ogino, and I.Shimada (2010).
NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode.
  J Biomol NMR, 48, 59-64.
PDB code: 2rr8
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