2axm

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[[Image:2axm.gif|left|200px]]
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{{STRUCTURE_2axm| PDB=2axm | SCENE= }}
{{STRUCTURE_2axm| PDB=2axm | SCENE= }}
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'''HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR'''
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===HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR===
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==Overview==
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The fibroblast growth factors (FGFs) form a large family of structurally related, multifunctional proteins that regulate various biological responses. They mediate cellular functions by binding to transmembrane FGF receptors, which are protein tyrosine kinases. FGF receptors are activated by oligomerization, and both this activation and FGF-stimulated biological responses require heparin-like molecules as well as FGF. Heparins are linear anionic polysaccharide chains; they are typically heterogeneously sulphated on alternating L-iduronic and D-glucosamino sugars, and are nearly ubiquitous in animal tissues as heparan sulphate proteoglycans on cell surfaces and in the extracellular matrix. Although several crystal structures have been described for FGF molecules in complexes with heparin-like sugars, the nature of a biologically active complex has been unknown until now. Here we describe the X-ray crystal structure, at 2.9 A resolution, of a biologically active dimer of human acidic FGF in a complex with a fully sulphated, homogeneous heparin decassacharide. The dimerization of heparin-linked acidic FGF observed here is an elegant mechanism for the modulation of signalling through combinatorial homodimerization and heterodimerization of the 12 known members of the FGF family.
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The line below this paragraph, {{ABSTRACT_PUBMED_9655399}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9655399 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9655399}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structure of a heparin-linked biologically active dimer of fibroblast growth factor., DiGabriele AD, Lax I, Chen DI, Svahn CM, Jaye M, Schlessinger J, Hendrickson WA, Nature. 1998 Jun 25;393(6687):812-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9655399 9655399]
Structure of a heparin-linked biologically active dimer of fibroblast growth factor., DiGabriele AD, Lax I, Chen DI, Svahn CM, Jaye M, Schlessinger J, Hendrickson WA, Nature. 1998 Jun 25;393(6687):812-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9655399 9655399]
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X-ray crystal structure of human acidic fibroblast growth factor., Blaber M, DiSalvo J, Thomas KA, Biochemistry. 1996 Feb 20;35(7):2086-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8652550 8652550]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hexagonal crystal form]]
[[Category: Hexagonal crystal form]]
[[Category: Human acidic fibroblast growth factor]]
[[Category: Human acidic fibroblast growth factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:35:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:40:17 2008''

Revision as of 09:40, 28 July 2008

Template:STRUCTURE 2axm

HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR

Template:ABSTRACT PUBMED 9655399

About this Structure

2AXM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a heparin-linked biologically active dimer of fibroblast growth factor., DiGabriele AD, Lax I, Chen DI, Svahn CM, Jaye M, Schlessinger J, Hendrickson WA, Nature. 1998 Jun 25;393(6687):812-7. PMID:9655399

X-ray crystal structure of human acidic fibroblast growth factor., Blaber M, DiSalvo J, Thomas KA, Biochemistry. 1996 Feb 20;35(7):2086-94. PMID:8652550

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