5kf4

From Proteopedia

(Difference between revisions)

Revision as of 08:50, 27 December 2017

Crystal structure of FN3 domain (Residues P368-P466) of Human collagen XX

Structural highlights

5kf4 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	COL20A1, KIAA1510 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COKA1_HUMAN] Probable collagen protein.

Publication Abstract from PubMed

Collagen alpha1 type XX, which contains fibronectin type III (FN3) repeats involving six FN3 domains (referred to as the FN#1-FN#6 domains), is an unusual member of the fibril-associated collagens with interrupted triple helices (FACIT) subfamily of collagens. The results of standard protein BLAST suggest that the FN3 repeats might contribute to collagen alpha1 type XX acting as a cytokine receptor. To date, solution NMR structures of the FN#3, FN#4 and FN#6 domains have been determined. To obtain further structural evidence to understand the relationship between the structure and function of the FN3 repeats from collagen alpha1 type XX, the crystal structure of the FN#2 domain from human collagen alpha1 type XX (residues Pro386-Pro466; referred to as FN2-HCXX) was solved at 2.5 A resolution. The crystal structure of FN2-HCXX shows an immunoglobulin-like fold containing a beta-sandwich structure, which is formed by a three-stranded beta-sheet (beta1, beta2 and beta5) packed onto a four-stranded beta-sheet (beta3, beta4, beta6 and beta7). Two consensus domains, tencon and fibcon, are structural analogues of FN2-HCXX. Fn8, an FN3 domain from human oncofoetal fibronectin, is the closest structural analogue of FN2-HCXX derived from a naturally occurring sequence. Based solely on the structural similarity of FN2-HCXX to other FN3 domains, the detailed functions of FN2-HCXX and the FN3 repeats in collagen alpha1 type XX cannot be identified.

Crystal structure of the second fibronectin type III (FN3) domain from human collagen alpha1 type XX.,Zhao J, Ren J, Wang N, Cheng Z, Yang R, Lin G, Guo Y, Cai D, Xie Y, Zhao X Acta Crystallogr F Struct Biol Commun. 2017 Dec 1;73(Pt 12):695-700. doi:, 10.1107/S2053230X1701648X. Epub 2017 Nov 21. PMID:29199991^[1]

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

References

↑ Zhao J, Ren J, Wang N, Cheng Z, Yang R, Lin G, Guo Y, Cai D, Xie Y, Zhao X. Crystal structure of the second fibronectin type III (FN3) domain from human collagen alpha1 type XX. Acta Crystallogr F Struct Biol Commun. 2017 Dec 1;73(Pt 12):695-700. doi:, 10.1107/S2053230X1701648X. Epub 2017 Nov 21. PMID:29199991 doi:http://dx.doi.org/10.1107/S2053230X1701648X

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5kf4"

@@ Line 3: / Line 3: @@
 <StructureSection load='5kf4' size='340' side='right' caption='[[5kf4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5kf4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KF4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5kf4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KF4 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kf4 OCA], [http://pdbe.org/5kf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kf4 RCSB], [http://www.ebi.ac.uk/pdbsum/5kf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kf4 ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COL20A1, KIAA1510 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kf4 OCA], [http://pdbe.org/5kf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kf4 RCSB], [http://www.ebi.ac.uk/pdbsum/5kf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kf4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 10: / Line 11: @@
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-The use of consensus design to produce stable proteins has been applied to numerous structures and classes of proteins. Here, we describe the engineering of novel FN3 domains from two different proteins, namely human fibronectin and human tenascin-C, as potential alternative scaffold biotherapeutics. The resulting FN3 domains were found to be robustly expressed in Escherichia coli, soluble and highly stable, with melting temperatures of 89 and 78 degrees C, respectively. X-ray crystallography was used to confirm that the consensus approach led to a structure consistent with the FN3 design despite having only low-sequence identity to natural FN3 domains. The ability of the Tenascin consensus domain to withstand mutations in the loop regions connecting the beta-strands was investigated using alanine scanning mutagenesis demonstrating the potential for randomization in these regions. Finally, rational design was used to produce point mutations that significantly increase the stability of one of the consensus domains. Together our data suggest that consensus FN3 domains have potential utility as alternative scaffold therapeutics.
+Collagen alpha1 type XX, which contains fibronectin type III (FN3) repeats involving six FN3 domains (referred to as the FN#1-FN#6 domains), is an unusual member of the fibril-associated collagens with interrupted triple helices (FACIT) subfamily of collagens. The results of standard protein BLAST suggest that the FN3 repeats might contribute to collagen alpha1 type XX acting as a cytokine receptor. To date, solution NMR structures of the FN#3, FN#4 and FN#6 domains have been determined. To obtain further structural evidence to understand the relationship between the structure and function of the FN3 repeats from collagen alpha1 type XX, the crystal structure of the FN#2 domain from human collagen alpha1 type XX (residues Pro386-Pro466; referred to as FN2-HCXX) was solved at 2.5 A resolution. The crystal structure of FN2-HCXX shows an immunoglobulin-like fold containing a beta-sandwich structure, which is formed by a three-stranded beta-sheet (beta1, beta2 and beta5) packed onto a four-stranded beta-sheet (beta3, beta4, beta6 and beta7). Two consensus domains, tencon and fibcon, are structural analogues of FN2-HCXX. Fn8, an FN3 domain from human oncofoetal fibronectin, is the closest structural analogue of FN2-HCXX derived from a naturally occurring sequence. Based solely on the structural similarity of FN2-HCXX to other FN3 domains, the detailed functions of FN2-HCXX and the FN3 repeats in collagen alpha1 type XX cannot be identified.
-Design of novel FN3 domains with high stability by a consensus sequence approach.,Jacobs SA, Diem MD, Luo J, Teplyakov A, Obmolova G, Malia T, Gilliland GL, O'Neil KT Protein Eng Des Sel. 2012 Mar;25(3):107-17. Epub 2012 Jan 12. PMID:22240293<ref>PMID:22240293</ref>
+Crystal structure of the second fibronectin type III (FN3) domain from human collagen alpha1 type XX.,Zhao J, Ren J, Wang N, Cheng Z, Yang R, Lin G, Guo Y, Cai D, Xie Y, Zhao X Acta Crystallogr F Struct Biol Commun. 2017 Dec 1;73(Pt 12):695-700. doi:, 10.1107/S2053230X1701648X. Epub 2017 Nov 21. PMID:29199991<ref>PMID:29199991</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Cheng, Z]]
 [[Category: Xie, Y]]

5kf4

From Proteopedia

Revision as of 08:50, 27 December 2017

Crystal structure of FN3 domain (Residues P368-P466) of Human collagen XX

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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