3zrz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3zrz.png|left|200px]]
 
- 
-
<!--
 
-
The line below this paragraph, containing "STRUCTURE_3zrz", creates the "Structure Box" on the page.
 
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
 
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
 
-
or leave the SCENE parameter empty for the default display.
 
-
-->
 
{{STRUCTURE_3zrz| PDB=3zrz | SCENE= }}
{{STRUCTURE_3zrz| PDB=3zrz | SCENE= }}
- 
===CRYSTAL STRUCTURE OF THE SECOND AND THIRD FIBRONECTIN F1 MODULES IN COMPLEX WITH A FRAGMENT OF STREPTOCOCCUS PYOGENES SFBI-5===
===CRYSTAL STRUCTURE OF THE SECOND AND THIRD FIBRONECTIN F1 MODULES IN COMPLEX WITH A FRAGMENT OF STREPTOCOCCUS PYOGENES SFBI-5===
 +
{{ABSTRACT_PUBMED_21840989}}
 +
==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==
-
The line below this paragraph, {{ABSTRACT_PUBMED_21840989}}, adds the Publication Abstract to the page
+
[[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>
-
(as it appears on PubMed at http://www.pubmed.gov), where 21840989 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_21840989}}
+
==About this Structure==
==About this Structure==
Line 22: Line 13:
==Reference==
==Reference==
-
<ref group="xtra">PMID:021840989</ref><references group="xtra"/>
+
<ref group="xtra">PMID:021840989</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bingham, R J.]]
[[Category: Bingham, R J.]]

Revision as of 16:13, 24 March 2013

Template:STRUCTURE 3zrz

Contents

CRYSTAL STRUCTURE OF THE SECOND AND THIRD FIBRONECTIN F1 MODULES IN COMPLEX WITH A FRAGMENT OF STREPTOCOCCUS PYOGENES SFBI-5

Template:ABSTRACT PUBMED 21840989

Disease

[FINC_HUMAN] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM: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.[1]

Function

[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.[2][3][4][5] 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.[6][7][8][9]

About this Structure

3zrz is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Norris NC, Bingham RJ, Harris G, Speakman A, Jones RP, Leech A, Turkenburg JP, Potts JR. Structural and functional analysis of the tandem {beta}-zipper interaction of a streptococcal protein with human fibronectin. J Biol Chem. 2011 Aug 12. PMID:21840989 doi:10.1074/jbc.M111.276592
  1. ↑ Castelletti F, Donadelli R, Banterla F, Hildebrandt F, Zipfel PF, Bresin E, Otto E, Skerka C, Renieri A, Todeschini M, Caprioli J, Caruso RM, Artuso R, Remuzzi G, Noris M. Mutations in FN1 cause glomerulopathy with fibronectin deposits. Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2538-43. Epub 2008 Feb 11. PMID:18268355 doi:0707730105
  2. ↑ Morla A, Zhang Z, Ruoslahti E. Superfibronectin is a functionally distinct form of fibronectin. Nature. 1994 Jan 13;367(6459):193-6. PMID:8114919 doi:http://dx.doi.org/10.1038/367193a0
  3. ↑ Yi M, Ruoslahti E. A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis. Proc Natl Acad Sci U S A. 2001 Jan 16;98(2):620-4. PMID:11209058 doi:10.1073/pnas.98.2.620
  4. ↑ Ambesi A, Klein RM, Pumiglia KM, McKeown-Longo PJ. Anastellin, a fragment of the first type III repeat of fibronectin, inhibits extracellular signal-regulated kinase and causes G(1) arrest in human microvessel endothelial cells. Cancer Res. 2005 Jan 1;65(1):148-56. PMID:15665290
  5. ↑ You R, Klein RM, Zheng M, McKeown-Longo PJ. Regulation of p38 MAP kinase by anastellin is independent of anastellin's effect on matrix fibronectin. Matrix Biol. 2009 Mar;28(2):101-9. doi: 10.1016/j.matbio.2009.01.003. Epub 2009, Feb 4. PMID:19379667 doi:10.1016/j.matbio.2009.01.003
  6. ↑ Morla A, Zhang Z, Ruoslahti E. Superfibronectin is a functionally distinct form of fibronectin. Nature. 1994 Jan 13;367(6459):193-6. PMID:8114919 doi:http://dx.doi.org/10.1038/367193a0
  7. ↑ Yi M, Ruoslahti E. A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis. Proc Natl Acad Sci U S A. 2001 Jan 16;98(2):620-4. PMID:11209058 doi:10.1073/pnas.98.2.620
  8. ↑ Ambesi A, Klein RM, Pumiglia KM, McKeown-Longo PJ. Anastellin, a fragment of the first type III repeat of fibronectin, inhibits extracellular signal-regulated kinase and causes G(1) arrest in human microvessel endothelial cells. Cancer Res. 2005 Jan 1;65(1):148-56. PMID:15665290
  9. ↑ You R, Klein RM, Zheng M, McKeown-Longo PJ. Regulation of p38 MAP kinase by anastellin is independent of anastellin's effect on matrix fibronectin. Matrix Biol. 2009 Mar;28(2):101-9. doi: 10.1016/j.matbio.2009.01.003. Epub 2009, Feb 4. PMID:19379667 doi:10.1016/j.matbio.2009.01.003

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zrz"
Personal tools