Clathrin

 

What InterPro Tells Us

P49951 Bovine clathrin heavy chain

 

InterPro Domain Architecture

 

InterPro Entry

Signatures

Graphical Match

IPR000547

PF00637

IPR000547

SM00299

IPR001473

PF01394

IPR011990

G3DSA:1.25.40.10

IPR015348

PF09268

Structural Features

 

 

 

1b89A

 

1utcA, 1utcB

1.25.40.10.18

1b89A00 

2.130.10.110.1

1utcA00 

a.118.1.3

d1b89a_ 

a.118.1.4

d1utca1 

b.69.6.1

d1utca2 

Structural Predictions

 

 

 

MB_P49951

 

SW_P49951 

 

From the graphical match in the table above, you can see that the signatures are grouped into four InterPro entries for bovine clathrin heavy chain.  These entries identify the domain architecture and sequence features of this protein. 

DOMAIN Entries

Ø      IPR001473: Clathrin propeller, N-terminal, represented by one signature: PF01394 (PFAM). 

Ø      IPR011990: Tetratricopeptide-like helical, represented by one signature: G3DSA:1.25.40.10 (Gene3D).

Ø      IPR015348: Clathrin heavy chain, linker, core motif, represented by one signature: PF09268 (PFAM).

REPEAT Entries

Ø      IPR000547: Clathrin heavy chain, 7-fold repeat, represented by two signatures: PF00637 (PFAM) and SM00299 (SMART). 

The bovine clathrin heavy chain consists of different repetitive sequence elements.  The N-terminal is composed of seven 4-stranded beta-sheet motifs that form a beta-propeller (IPR001473).  The beta-propeller is at the tip of each leg of the triskelion, and is responsible for binding clathrin adaptors and membrane attachment proteins.  The linker region (IPR015348) is a short alpha-helical sequence (ARM-repeat-like) linking the N- and C-terminal domains.  The C-terminal is composed of a 7-fold tetratricopeptide repeat (alpha-alpha-superhelical ARM-repeat) with a similar structure to the short linker region.  The C-terminal forms the central hub of the triskelion.

 

Structural features

The remaining ten entries in the table above give information on the known and predicted structure of this protein.  These entries present known structural data from the structural database PDB (green stripe) and the structural classification databases CATH (pink stripe) and SCOP (black stripe) (the names such as 1b89A00 are derived from the PDB entry upon which they are based, here PDB entry 1b89, chain A), as well as predicted structural data from the homology model databases ModBase (yellow stripe) and Swiss-Model (red stripe).

  The graphical matches for the PDB entries 1utc and 1b89 display the full-length original PDB entries for the N- and C-terminal regions, respectively.  Both CATH (1b89A00) and SCOP (d1b89a_) classify the C-terminal region as an ARM repeat alpha-alpha-superhelical structure, but they differ in their classification of the N-terminal region.  CATH (1utcA00) classifies the entire N-terminal structure as an beta-propeller, while SCOP (d1utca1; d1utca2) divides it into an N-terminal beta-propeller, and a short ARM repeat alpha-helical linker.

The homology models from both ModBase (MB_P49951) and Swiss-Model (SW_P49951) cover a larger portion of the N-terminal region of the clathrin heavy chain.

 

What the Structure Tells Us

 

            Structures associated with the bovine clathrin heavy chain can be viewed using AstexViewer®, which is linked from the Match Table via the logo  on the InterPro page (please note, there is no link directly from this page to the AstexViewer®, therefore you need to go to the  link on the InterPro page for P49951).  The AstexViewer® displays the PDB structure with the CATH or SCOP domain highlighted in yellow.  In the picture below, the SCOP domain representing the N-terminal region is shown.  Note that there are two copies of the N-terminal (i.e. shown as a dimer); the beta-sheet structure in yellow represents the N-terminal beta-propeller, while the short helix in green to its left represents the short helical linker region (the entire N-terminal structure is repeated in green on the right).

 

 

 

AstexView of bovine clathrin heavy chain, N-terminal region:  the beta-propeller is shown in yellow, while the short alpha-helical linker is to its left in green; the region is duplicated in green on the right (i.e. shown as a dimer).


           

There are structures available for several clathrin heavy chains from different organisms in the Protein Data Bank (PDB).  A detailed description and visualisation of the structural features of clathrin can be found at the PDB ‘Molecule of the Month’.  The crystallographic structures of clathrin lattices have provided insight into clathrin-mediated protein transport.

 

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