1evt: Difference between revisions

Revision as of 02:06, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1evt.png

Template:STRUCTURE 1evt

CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)

Template:ABSTRACT PUBMED 10830168

About this StructureAbout this Structure

1EVT is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity., Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M, Cell. 2000 May 12;101(4):413-24. PMID:10830168

Page seeded by OCA on Tue Jul 1 02:06:02 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1evt.gif|left|200px]]
+{{Seed}}
+[[Image:1evt.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1evt|  PDB=1evt  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)'''
+===CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)===
-==Overview==
+<!--
-To elucidate the structural determinants governing specificity in fibroblast growth factor (FGF) signaling, we have determined the crystal structures of FGF1 and FGF2 complexed with the ligand binding domains (immunoglobulin-like domains 2 [D2] and 3 [D3]) of FGF receptor 1 (FGFR1) and FGFR2, respectively. Highly conserved FGF-D2 and FGF-linker (between D2-D3) interfaces define a general binding site for all FGF-FGFR complexes. Specificity is achieved through interactions between the N-terminal and central regions of FGFs and two loop regions in D3 that are subject to alternative splicing. These structures provide a molecular basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR specificity through primary sequence variations and alternative splicing.
+The line below this paragraph, {{ABSTRACT_PUBMED_10830168}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10830168 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10830168}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Schlessinger, J.]]
 [[Category: B-trefoil fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:34:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:06:02 2008''