PDBsum entry 2ki6

Protein transport

PDB id: 2ki6

Contents

Protein chains

128 a.a. *

133 a.a. *

98 a.a. *

* Residue conservation analysis

PDB id:

2ki6

Name:

Protein transport

Title:

The fgf1-s100a13-c2a hetero-hexameric complex structure: a component in the non-classical pathway for fgf1 secretion

Structure:

Synaptotagmin-1. Chain: a, f. Fragment: c2a domain. Synonym: synaptotagmin i, syti, p65. Engineered: yes. Heparin-binding growth factor 1. Chain: b, e. Synonym: hbgf-1, acidic fibroblast growth factor, afgf, beta- endothelial cell growth factor, ecgf-beta.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: syt1, svp65, syt. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: purified from heparin affinity column. Gene: fgf1, fgfa. Other_details: purified from gst column.

NMR struc:

18 models

Authors:

S.M.Krishna,S.G.Rani,C.Yu

Key ref:

S.K.Mohan et al. (2010). The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion. J Biol Chem, 285, 15464-15475. PubMed id: 20220137

Date:

28-Apr-09 Release date: 09-Mar-10

Protein chains

P21579  (SYT1_HUMAN) -  Synaptotagmin-1 from Homo sapiens

Seq: 422 a.a.

Struc: 128 a.a.

Protein chains

P05230  (FGF1_HUMAN) -  Fibroblast growth factor 1 from Homo sapiens

Seq: 155 a.a.

Struc: 133 a.a.

Protein chains

Q99584  (S10AD_HUMAN) -  Protein S100-A13 from Homo sapiens

Seq: 98 a.a.

Struc: 98 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

J Biol Chem 285:15464-15475 (2010)

PubMed id: 20220137

The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion.

S.K.Mohan, S.G.Rani, C.Yu.

ABSTRACT

Fibroblast growth factors (FGFs) are key regulators of cell proliferation, tumor-induced angiogenesis, and migration. FGFs are essential for early embryonic development, organ formation, and angiogenesis. FGF1 also plays an important role in inflammation, wound healing, and restenosis. The biological effects of FGF1 are mediated through the activation of the four transmembrane phosphotyrosine kinase fibroblast growth factor receptors in the presence of heparin sulfate proteoglycans and, therefore, require the release of the protein into the extracellular space. FGF1 is exported through a non-classical release pathway involving the formation of a specific multiprotein complex. The protein constituents of this complex include FGF1, S100A13, and the p40 form of synaptotagmin 1 (Syt1). Because FGF1 plays an important role in tumor formation, it is clear that preventing the formation of the multiprotein complex would be an effective strategy to inhibit a wide range of cancers. To understand the molecular events in the FGF1 release pathway, we studied the FGF1-S100A13 tetrameric and FGF1-S100A13-C2A hexameric complex structures, which are both complexes possibly formed during the non-classical pathway of FGF1 release.