4pz5: Difference between revisions

Line 1:

'''~~Unreleased structure~~'''

==Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of BBK32 from Borrelia burgdorferi==

~~The entry~~ 4pz5 is ~~ON HOLD until Paper Publication~~

== Structural highlights ==

<table><tr><td colspan='2'>[[4pz5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZ5 FirstGlance]. <br>

~~Authors~~: ~~Harris~~, G., ~~Potts~~, J.R.

</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pz5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pz5 RCSB], [http://www.ebi.ac.uk/pdbsum/4pz5 PDBsum]</span></td></tr>

~~Description~~: ~~Crystal structure~~ of the second and ~~third fibronectin F1 modules~~ in ~~complex with a fragment~~ of ~~BBK32 from Borrelia burgdorferi~~

<table>

== Disease ==

[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[http://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref>

== Function ==

[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Harris, G.]]

[[Category: Potts, J R.]]

[[Category: Bacterial adhesion]]

[[Category: Cell adhesion]]

[[Category: Extracellular matrix]]

[[Category: Fibronectin binding]]

[[Category: Fibronectin type one]]

[[Category: Plasma]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of BBK32 from Borrelia burgdorferi==
+<StructureSection load='4pz5' size='340' side='right' caption='[[4pz5]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
-The entry 4pz5 is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4pz5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZ5 FirstGlance]. <br>
-Authors: Harris, G., Potts, J.R.
+</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pz5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pz5 RCSB], [http://www.ebi.ac.uk/pdbsum/4pz5 PDBsum]</span></td></tr>
-Description: Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of BBK32 from Borrelia burgdorferi
+<table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[http://omim.org/entry/601894 601894]]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref>
+== Function ==
+[[http://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN]] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref>   Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Harris, G.]]
+[[Category: Potts, J R.]]
+[[Category: Bacterial adhesion]]
+[[Category: Cell adhesion]]
+[[Category: Extracellular matrix]]
+[[Category: Fibronectin binding]]
+[[Category: Fibronectin type one]]
+[[Category: Plasma]]