This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1fmm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:29, 22 May 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1fmm.gif|left|200px]]
 
-
{{Structure
+
==SOLUTION STRUCTURE OF NFGF-1==
-
|PDB= 1fmm |SIZE=350|CAPTION= <scene name='initialview01'>1fmm</scene>
+
<StructureSection load='1fmm' size='340' side='right'caption='[[1fmm]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1fmm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Notophthalmus_viridescens Notophthalmus viridescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMM FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmm OCA], [https://pdbe.org/1fmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmm RCSB], [https://www.ebi.ac.uk/pdbsum/1fmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmm ProSAT]</span></td></tr>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmm OCA], [http://www.ebi.ac.uk/pdbsum/1fmm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fmm RCSB]</span>
+
[https://www.uniprot.org/uniprot/FGF1_NOTVI FGF1_NOTVI] Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro (By similarity).
-
}}
+
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fmm_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fmm ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The three-dimensional solution structure of an acidic fibroblast growth factor (nFGF-1) from the newt (Notophthalmus viridescens) is determined using multidimensional NMR techniques. Complete assignment of all the atoms ((1)H, (15)N, and (13)C) has been achieved using a variety of triple resonance experiments. 50 structures were calculated using hybrid distance geometry-dynamical simulated annealing technique with a total of 1359 constraints. The atomic root mean square distribution for the backbone atoms in the structured region is 0.60 A. The secondary structural elements include 12 beta-strands arranged antiparallely into a beta-barrel structure. The protein (nFGF-1) exists in a monomeric state upon binding to the ligand, sucrose octa sulfate (SOS), in a stoichiometric ratio of 1:1. The SOS binding site consists of a dense cluster of positively charged residues located at the C-terminal end of the molecule. The conformational stabilities of nFGF-1 and its structural and functional homologue from the human source (hFGF-1) are drastically different. The differential stabilities of nFGF-1 and hFGF-1 are attributed to the differences in the number of hydrogen bonds and the presence of solvent inaccessible cavities in the two proteins.
-
'''SOLUTION STRUCTURE OF NFGF-1'''
+
Structure and stability of an acidic fibroblast growth factor from Notophthalmus viridescens.,Arunkumar AI, Srisailam S, Kumar TK, Kathir KM, Chi YH, Wang HM, Chang GG, Chiu I, Yu C J Biol Chem. 2002 Nov 29;277(48):46424-32. Epub 2002 Aug 29. PMID:12205097<ref>PMID:12205097</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1fmm" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The three-dimensional solution structure of an acidic fibroblast growth factor (nFGF-1) from the newt (Notophthalmus viridescens) is determined using multidimensional NMR techniques. Complete assignment of all the atoms ((1)H, (15)N, and (13)C) has been achieved using a variety of triple resonance experiments. 50 structures were calculated using hybrid distance geometry-dynamical simulated annealing technique with a total of 1359 constraints. The atomic root mean square distribution for the backbone atoms in the structured region is 0.60 A. The secondary structural elements include 12 beta-strands arranged antiparallely into a beta-barrel structure. The protein (nFGF-1) exists in a monomeric state upon binding to the ligand, sucrose octa sulfate (SOS), in a stoichiometric ratio of 1:1. The SOS binding site consists of a dense cluster of positively charged residues located at the C-terminal end of the molecule. The conformational stabilities of nFGF-1 and its structural and functional homologue from the human source (hFGF-1) are drastically different. The differential stabilities of nFGF-1 and hFGF-1 are attributed to the differences in the number of hydrogen bonds and the presence of solvent inaccessible cavities in the two proteins.
+
*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1FMM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Notophthalmus_viridescens Notophthalmus viridescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMM OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
Structure and stability of an acidic fibroblast growth factor from Notophthalmus viridescens., Arunkumar AI, Srisailam S, Kumar TK, Kathir KM, Chi YH, Wang HM, Chang GG, Chiu I, Yu C, J Biol Chem. 2002 Nov 29;277(48):46424-32. Epub 2002 Aug 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12205097 12205097]
+
[[Category: Notophthalmus viridescens]]
[[Category: Notophthalmus viridescens]]
-
[[Category: Single protein]]
+
[[Category: Arunkumar AI]]
-
[[Category: Arunkumar, A I.]]
+
[[Category: Chiu IM]]
-
[[Category: Chiu, I M.]]
+
[[Category: Kumar TKS]]
-
[[Category: Kumar, T K.S.]]
+
[[Category: Srisailam S]]
-
[[Category: Srisailam, S.]]
+
[[Category: Yu C]]
-
[[Category: Yu, C.]]
+
-
[[Category: growth factor]]
+
-
[[Category: mitogen]]
+
-
[[Category: triple resonance]]
+
-
[[Category: wound healing]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:25:56 2008''
+

Current revision

SOLUTION STRUCTURE OF NFGF-1

PDB ID 1fmm

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools