Database accession: MF7000697
Name: Pacsin2
PDB ID: 4bne
Experimental method: X-ray (2.57 Å)
Assembly: Homodimer
Source organism: Gallus gallus
Primary publication of the structure:
Kostan J, Salzer U, Orlova A, Törö I, Hodnik V, Senju Y, Zou J, Schreiner C, Steiner J, Meriläinen J, Nikki M, Virtanen I, Carugo O, Rappsilber J, Lappalainen P, Lehto VP, Anderluh G, Egelman EH, Djinović-Carugo K
Direct interaction of actin filaments with F-BAR protein pacsin2.
(2014) EMBO Rep. 15: 1154-62
PMID: 25216944
Abstract:
Two mechanisms have emerged as major regulators of membrane shape: BAR domain-containing proteins, which induce invaginations and protrusions, and nuclear promoting factors, which cause generation of branched actin filaments that exert mechanical forces on membranes. While a large body of information exists on interactions of BAR proteins with membranes and regulatory proteins of the cytoskeleton, little is known about connections between these two processes. Here, we show that the F-BAR domain protein pacsin2 is able to associate with actin filaments using the same concave surface employed to bind to membranes, while some other tested N-BAR and F-BAR proteins (endophilin, CIP4 and FCHO2) do not associate with actin. This finding reveals a new level of complexity in membrane remodeling processes.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
cytoskeletal protein binding cytoskeletal protein binding
phosphatidic acid binding phosphatidic acid binding
phospholipid binding phospholipid binding
Biological process:
actin cytoskeleton organization actin cytoskeleton organization
caveola assembly caveola assembly
cytoskeleton organization cytoskeleton organization
endocytosis endocytosis
negative regulation of endocytosis negative regulation of endocytosis
plasma membrane tubulation plasma membrane tubulation
regulation of endocytosis regulation of endocytosis
Cellular component:
caveola caveola
cytoplasm cytoplasm
cytoskeleton cytoskeleton
cytosol cytosol
early endosome early endosome
endosome endosome
focal adhesion focal adhesion
plasma membrane plasma membrane
recycling endosome membrane recycling endosome membrane
ruffle membrane ruffle membrane
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Protein kinase C and casein kinase substrate in neurons protein 2
Source organism: Gallus gallus
Length: 448 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKKKASDGVTLTGINQTGDQVSQPNKHSSVSSYEKNQSYPTDWSDEESNNPFSSTDAKGDTNPFDEDTSPVMEVRVRALYDYEGQEQDELSFKAGDELTKMENEDEQGWCKGRLDNGQVGLYPANYVEPIQ
UniProtKB AC: O13154 (positions: 15-304)
Coverage: 64%
Name: Protein kinase C and casein kinase substrate in neurons protein 2
Source organism: Gallus gallus
Length: 448 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKKKASDGVTLTGINQTGDQVSQPNKHSSVSSYEKNQSYPTDWSDEESNNPFSSTDAKGDTNPFDEDTSPVMEVRVRALYDYEGQEQDELSFKAGDELTKMENEDEQGWCKGRLDNGQVGLYPANYVEPIQ
UniProtKB AC: O13154 (positions: 15-303)
Coverage: 64%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: F-BAR domain
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
F-BAR domains form an intimately packed six-helix bundle and bury a large, hydrophobic dimerization interface. They exist as dimers in solution, with no evidence for monomeric forms (PMID:17512409). Other BAR domains (N-BAR) displayed a two-state equilibrium unfolding (PMID:26368922, PMID:34423187).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
