1k5u: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1k5u.gif|left|200px]]<br /><applet load="1k5u" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1k5u.gif|left|200px]]
caption="1k5u, resolution 2.0&Aring;" />
 
'''Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with His93 replaced by Gly (H93G).'''<br />
{{Structure
|PDB= 1k5u |SIZE=350|CAPTION= <scene name='initialview01'>1k5u</scene>, resolution 2.0&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY=
|GENE=
}}
 
'''Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with His93 replaced by Gly (H93G).'''
 


==Overview==
==Overview==
Line 10: Line 19:


==About this Structure==
==About this Structure==
1K5U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5U OCA].  
1K5U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5U OCA].  


==Reference==
==Reference==
Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor., Kim J, Blaber SI, Blaber M, Protein Sci. 2002 Mar;11(3):459-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11847269 11847269]
Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor., Kim J, Blaber SI, Blaber M, Protein Sci. 2002 Mar;11(3):459-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11847269 11847269]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 22: Line 31:
[[Category: beta-trefoil]]
[[Category: beta-trefoil]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:32 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:13:00 2008''

Revision as of 13:13, 20 March 2008

File:1k5u.gif


PDB ID 1k5u

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with His93 replaced by Gly (H93G).


OverviewOverview

Human acidic fibroblast growth factor (FGF-1) has a beta-trefoil structure, one of the fundamental protein superfolds. The X-ray crystal structures of wild-type and various mutant forms of FGF-1 have been solved in five different space groups: C2, C222(1), P2(1) (four molecules/asu), P2(1) (three molecules/asu), and P2(1)2(1)2(1). These structures reveal two characteristically different conformations for the beta8/beta9 beta-hairpin comprising residue positions 90-94. This region in the wild-type FGF-1 structure (P2(1), four molecules/asu), a his-tagged His93-->Gly mutant (P2(1), three molecules/asu) and a his-tagged Asn106-->Gly mutant (P2(1)2(1)2(1)) adopts a 3:5 beta-hairpin known as a type I (1-4) G1 beta-bulge (containing a type I turn). However, a his-tagged form of wild-type FGF-1 (C222(1)) and a his-tagged Leu44-->Phe mutant (C2) adopt a 3:3 beta-hairpin (containing a type I' turn) for this same region. A feature that distinguishes these two types of beta-hairpin structures is the number and location of side chain positions with eclipsed C(beta) and main-chain carbonyl oxygen groups (Psi is equivalent to +60 degrees). The effects of glycine mutations upon stability, at positions within the hairpin, have been used to identify the most likely structure in solution. Type I' turns in the structural data bank are quite rare, and a survey of these turns reveals that a large percentage exhibit crystal contacts within 3.0 A. This suggests that many of the type I' turns in X-ray structures may be adopted due to crystal packing effects.

DiseaseDisease

Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[602115], LADD syndrome OMIM:[602115]

About this StructureAbout this Structure

1K5U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor., Kim J, Blaber SI, Blaber M, Protein Sci. 2002 Mar;11(3):459-66. PMID:11847269

Page seeded by OCA on Thu Mar 20 12:13:00 2008

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

OCA