2uus: Difference between revisions

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[[Image:2uus.jpg|left|200px]]
{{Seed}}
[[Image:2uus.png|left|200px]]


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{{STRUCTURE_2uus|  PDB=2uus  |  SCENE=  }}  
{{STRUCTURE_2uus|  PDB=2uus  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE RAT FGF1-SUCROSE OCTASULFATE (SOS) COMPLEX.'''
===CRYSTAL STRUCTURE OF THE RAT FGF1-SUCROSE OCTASULFATE (SOS) COMPLEX.===




==Overview==
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Fibroblast growth factors (FGFs) constitute a family of at least 23 structurally related heparin-binding proteins that are involved in regulation of cell growth, survival, differentiation and migration. Sucrose octasulfate (SOS), a chemical analogue of heparin, has been demonstrated to activate FGF signalling pathways. The structure of rat FGF1 crystallized in the presence of SOS has been determined at 2.2 A resolution. SOS-mediated dimerization of FGF1 was observed, which was further supported by gel-filtration experiments. The major contributors to the sulfate-binding sites in rat FGF1 are Lys113, Lys118, Arg122 and Lys128. An arginine at position 116 is a consensus residue in mammalian FGF molecules; however, it is a serine in rat FGF1. This difference may be important for SOS-mediated FGF1 dimerization in rat.
The line below this paragraph, {{ABSTRACT_PUBMED_18540049}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18540049 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18540049}}


==About this Structure==
==About this Structure==
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[[Category: Mitogen]]
[[Category: Mitogen]]
[[Category: Sucrose octasulfate]]
[[Category: Sucrose octasulfate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:17:34 2008''
 
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