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. 2016 Sep 16;56(4):383–393. doi: 10.1007/s12088-016-0618-0

Fig. 2.

Fig. 2

Schematic representation of gelatin binding proteins (GBPs) structure based on the sequences and data available in uniprot site (http://www.uniprot.org/). a BSP Protein (PDC-109) contains two gelatin binding domains fn2A and fn2B, which are connected with linker chain (LC) of 7–9 amino acids. Two disulphide bonds (⋯S–S⋯) are present in each domain. b MMP-2 and c MMP-9 carry three gelatin binding domains at N terminal, which are tandemly arranged as fn2A, fn2B and fn2C and they are joined with each other by LC. Their C-terminal contains four hemopexin domains also d ELSPBP1 is a long fn2 domain containing protein. Each all four domains have two disulphide bonds. fn2A domain of GBPs is followed by N terminal and signal peptides. There is no LC between fn2A and fn2B domain in ELSPBP1. The uniprot identification numbers of these proteins are UniProtKB-P02784 for BSP protein (PDC-109), UniProtKB-P08253 for MMP-2, UniProtKB-P14780 for MMP-9 and UniProtKB-Q7YR83 for ELSPBP1