1qr4: Difference between revisions

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[[Image:1qr4.png|left|200px]]


{{STRUCTURE_1qr4| PDB=1qr4 | SCENE= }}
==TWO FIBRONECTIN TYPE-III DOMAIN SEGMENT FROM CHICKEN TENASCIN==
<StructureSection load='1qr4' size='340' side='right'caption='[[1qr4]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qr4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QR4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qr4 OCA], [https://pdbe.org/1qr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qr4 RCSB], [https://www.ebi.ac.uk/pdbsum/1qr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qr4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TENA_CHICK TENA_CHICK] Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.
== 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/qr/1qr4_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=1qr4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A fragment of chicken tenascin consisting of fibronectin type-III domains 5 and 6 has been expressed in Escherichia coli. After modifying a previously reported purification protocol, an electrophoretically homogeneous recombinant protein was obtained from which various crystal forms could be grown under identical conditions. Only one form was suitable for structure determination. These crystals belong to space group P21, with unit-cell parameters a = 45.2, b = 57.9, c = 72.2 A, beta = 91.4 degrees, and diffract to at least 2.6 A resolution using synchrotron radiation. From density measurements of the crystals, it was found that there are two molecules in the asymmetric unit. Diffraction data of native, two platinum-derivative and one palladium-derivative crystals were collected.


===TWO FIBRONECTIN TYPE-III DOMAIN SEGMENT FROM CHICKEN TENASCIN===
Purification, crystallization and preliminary crystallographic studies of a two fibronectin type-III domain segment from chicken tenascin encompassing the heparin- and contactin-binding regions.,Bisig D, Weber P, Vaughan L, Winterhalter KH, Piontek K Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1069-73. PMID:10216309<ref>PMID:10216309</ref>


{{ABSTRACT_PUBMED_10216309}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1qr4" style="background-color:#fffaf0;"></div>
[[1qr4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QR4 OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:010216309</ref><references group="xtra"/>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Bisig, D A.]]
[[Category: Large Structures]]
[[Category: Piontek, K.]]
[[Category: Bisig DA]]
[[Category: Adhesion]]
[[Category: Piontek K]]
[[Category: Extracellular matrix]]
[[Category: Fibronectin type-iii]]
[[Category: Fusion protein]]
[[Category: Heparin]]
[[Category: Structural protein]]
[[Category: Tenascin]]

Latest revision as of 13:05, 16 August 2023

TWO FIBRONECTIN TYPE-III DOMAIN SEGMENT FROM CHICKEN TENASCINTWO FIBRONECTIN TYPE-III DOMAIN SEGMENT FROM CHICKEN TENASCIN

Structural highlights

1qr4 is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.55Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TENA_CHICK Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A fragment of chicken tenascin consisting of fibronectin type-III domains 5 and 6 has been expressed in Escherichia coli. After modifying a previously reported purification protocol, an electrophoretically homogeneous recombinant protein was obtained from which various crystal forms could be grown under identical conditions. Only one form was suitable for structure determination. These crystals belong to space group P21, with unit-cell parameters a = 45.2, b = 57.9, c = 72.2 A, beta = 91.4 degrees, and diffract to at least 2.6 A resolution using synchrotron radiation. From density measurements of the crystals, it was found that there are two molecules in the asymmetric unit. Diffraction data of native, two platinum-derivative and one palladium-derivative crystals were collected.

Purification, crystallization and preliminary crystallographic studies of a two fibronectin type-III domain segment from chicken tenascin encompassing the heparin- and contactin-binding regions.,Bisig D, Weber P, Vaughan L, Winterhalter KH, Piontek K Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1069-73. PMID:10216309[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Bisig D, Weber P, Vaughan L, Winterhalter KH, Piontek K. Purification, crystallization and preliminary crystallographic studies of a two fibronectin type-III domain segment from chicken tenascin encompassing the heparin- and contactin-binding regions. Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1069-73. PMID:10216309

1qr4, resolution 2.55Å

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