2ys3

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the PH domain of Kindlin-3 from human

Structural highlights

2ys3 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Disease

URP2_HUMAN Leukocyte adhesion deficiency type III. The disease is caused by mutations affecting the gene represented in this entry.^[1] ^[2] ^[3] ^[4] ^[5]

Function

URP2_HUMAN Plays a central role in cell adhesion in hematopoietic cells. Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells. Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity).^[6] ^[7] ^[8] ^[9] Isoform 2 may act as a repressor of NF-kappa-B and apoptosis.^[10] ^[11] ^[12] ^[13]

Evolutionary Conservation

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

References

↑ Kuijpers TW, van de Vijver E, Weterman MA, de Boer M, Tool AT, van den Berg TK, Moser M, Jakobs ME, Seeger K, Sanal O, Unal S, Cetin M, Roos D, Verhoeven AJ, Baas F. LAD-1/variant syndrome is caused by mutations in FERMT3. Blood. 2009 May 7;113(19):4740-6. doi: 10.1182/blood-2008-10-182154. Epub 2008, Dec 8. PMID:19064721 doi:http://dx.doi.org/10.1182/blood-2008-10-182154
↑ Svensson L, Howarth K, McDowall A, Patzak I, Evans R, Ussar S, Moser M, Metin A, Fried M, Tomlinson I, Hogg N. Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nat Med. 2009 Mar;15(3):306-12. doi: 10.1038/nm.1931. Epub 2009 Feb 22. PMID:19234463 doi:http://dx.doi.org/10.1038/nm.1931
↑ Malinin NL, Zhang L, Choi J, Ciocea A, Razorenova O, Ma YQ, Podrez EA, Tosi M, Lennon DP, Caplan AI, Shurin SB, Plow EF, Byzova TV. A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nat Med. 2009 Mar;15(3):313-8. doi: 10.1038/nm.1917. Epub 2009 Feb 22. PMID:19234460 doi:http://dx.doi.org/10.1038/nm.1917
↑ Mory A, Feigelson SW, Yarali N, Kilic SS, Bayhan GI, Gershoni-Baruch R, Etzioni A, Alon R. Kindlin-3: a new gene involved in the pathogenesis of LAD-III. Blood. 2008 Sep 15;112(6):2591. doi: 10.1182/blood-2008-06-163162. PMID:18779414 doi:http://dx.doi.org/10.1182/blood-2008-06-163162
↑ Manevich-Mendelson E, Feigelson SW, Pasvolsky R, Aker M, Grabovsky V, Shulman Z, Kilic SS, Rosenthal-Allieri MA, Ben-Dor S, Mory A, Bernard A, Moser M, Etzioni A, Alon R. Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions. Blood. 2009 Sep 10;114(11):2344-53. doi: 10.1182/blood-2009-04-218636. Epub 2009 , Jul 17. PMID:19617577 doi:http://dx.doi.org/10.1182/blood-2009-04-218636
↑ Wang L, Deng W, Shi T, Ma D. URP2SF, a FERM and PH domain containing protein, regulates NF-kappaB and apoptosis. Biochem Biophys Res Commun. 2008 Apr 18;368(4):899-906. doi:, 10.1016/j.bbrc.2008.02.024. Epub 2008 Feb 14. PMID:18280249 doi:http://dx.doi.org/10.1016/j.bbrc.2008.02.024
↑ Kuijpers TW, van de Vijver E, Weterman MA, de Boer M, Tool AT, van den Berg TK, Moser M, Jakobs ME, Seeger K, Sanal O, Unal S, Cetin M, Roos D, Verhoeven AJ, Baas F. LAD-1/variant syndrome is caused by mutations in FERMT3. Blood. 2009 May 7;113(19):4740-6. doi: 10.1182/blood-2008-10-182154. Epub 2008, Dec 8. PMID:19064721 doi:http://dx.doi.org/10.1182/blood-2008-10-182154
↑ Svensson L, Howarth K, McDowall A, Patzak I, Evans R, Ussar S, Moser M, Metin A, Fried M, Tomlinson I, Hogg N. Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nat Med. 2009 Mar;15(3):306-12. doi: 10.1038/nm.1931. Epub 2009 Feb 22. PMID:19234463 doi:http://dx.doi.org/10.1038/nm.1931
↑ Malinin NL, Zhang L, Choi J, Ciocea A, Razorenova O, Ma YQ, Podrez EA, Tosi M, Lennon DP, Caplan AI, Shurin SB, Plow EF, Byzova TV. A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nat Med. 2009 Mar;15(3):313-8. doi: 10.1038/nm.1917. Epub 2009 Feb 22. PMID:19234460 doi:http://dx.doi.org/10.1038/nm.1917
↑ Wang L, Deng W, Shi T, Ma D. URP2SF, a FERM and PH domain containing protein, regulates NF-kappaB and apoptosis. Biochem Biophys Res Commun. 2008 Apr 18;368(4):899-906. doi:, 10.1016/j.bbrc.2008.02.024. Epub 2008 Feb 14. PMID:18280249 doi:http://dx.doi.org/10.1016/j.bbrc.2008.02.024
↑ Kuijpers TW, van de Vijver E, Weterman MA, de Boer M, Tool AT, van den Berg TK, Moser M, Jakobs ME, Seeger K, Sanal O, Unal S, Cetin M, Roos D, Verhoeven AJ, Baas F. LAD-1/variant syndrome is caused by mutations in FERMT3. Blood. 2009 May 7;113(19):4740-6. doi: 10.1182/blood-2008-10-182154. Epub 2008, Dec 8. PMID:19064721 doi:http://dx.doi.org/10.1182/blood-2008-10-182154
↑ Svensson L, Howarth K, McDowall A, Patzak I, Evans R, Ussar S, Moser M, Metin A, Fried M, Tomlinson I, Hogg N. Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nat Med. 2009 Mar;15(3):306-12. doi: 10.1038/nm.1931. Epub 2009 Feb 22. PMID:19234463 doi:http://dx.doi.org/10.1038/nm.1931
↑ Malinin NL, Zhang L, Choi J, Ciocea A, Razorenova O, Ma YQ, Podrez EA, Tosi M, Lennon DP, Caplan AI, Shurin SB, Plow EF, Byzova TV. A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nat Med. 2009 Mar;15(3):313-8. doi: 10.1038/nm.1917. Epub 2009 Feb 22. PMID:19234460 doi:http://dx.doi.org/10.1038/nm.1917

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ys3"

@@ Line 1: / Line 1: @@
 ==Solution structure of the PH domain of Kindlin-3 from human==
-<StructureSection load='2ys3' size='340' side='right'caption='[[2ys3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2ys3' size='340' side='right'caption='[[2ys3]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ys3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YS3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ys3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YS3 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">URP2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2ys3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ys3 OCA], [https://pdbe.org/2ys3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ys3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ys3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ys3 ProSAT], [https://www.topsan.org/Proteins/RSGI/2ys3 TOPSAN]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/URP2_HUMAN URP2_HUMAN]] Leukocyte adhesion deficiency type III. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:19064721</ref> <ref>PMID:19234463</ref> <ref>PMID:19234460</ref> <ref>PMID:18779414</ref> <ref>PMID:19617577</ref>
+[https://www.uniprot.org/uniprot/URP2_HUMAN URP2_HUMAN] Leukocyte adhesion deficiency type III. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:19064721</ref> <ref>PMID:19234463</ref> <ref>PMID:19234460</ref> <ref>PMID:18779414</ref> <ref>PMID:19617577</ref>
 == Function ==
-[[https://www.uniprot.org/uniprot/URP2_HUMAN URP2_HUMAN]] Plays a central role in cell adhesion in hematopoietic cells. Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells. Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity).<ref>PMID:18280249</ref> <ref>PMID:19064721</ref> <ref>PMID:19234463</ref> <ref>PMID:19234460</ref>   Isoform 2 may act as a repressor of NF-kappa-B and apoptosis.<ref>PMID:18280249</ref> <ref>PMID:19064721</ref> <ref>PMID:19234463</ref> <ref>PMID:19234460</ref>
+[https://www.uniprot.org/uniprot/URP2_HUMAN URP2_HUMAN] Plays a central role in cell adhesion in hematopoietic cells. Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells. Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity).<ref>PMID:18280249</ref> <ref>PMID:19064721</ref> <ref>PMID:19234463</ref> <ref>PMID:19234460</ref>   Isoform 2 may act as a repressor of NF-kappa-B and apoptosis.<ref>PMID:18280249</ref> <ref>PMID:19064721</ref> <ref>PMID:19234463</ref> <ref>PMID:19234460</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Harada, T]]
+[[Category: Harada T]]
-[[Category: Kigawa, T]]
+[[Category: Kigawa T]]
-[[Category: Koshiba, S]]
+[[Category: Koshiba S]]
-[[Category: Li, H]]
+[[Category: Li H]]
-[[Category: Structural genomic]]
+[[Category: Sato M]]
-[[Category: Sato, M]]
+[[Category: Watanabe S]]
-[[Category: Watanabe, S]]
+[[Category: Yokoyama S]]
-[[Category: Yokoyama, S]]
-[[Category: Kindlin-3]]
-[[Category: National project on protein structural and functional analyse]]
-[[Category: Nppsfa]]
-[[Category: Ph domain]]
-[[Category: Rsgi]]
-[[Category: Signaling protein]]
-[[Category: Unc-112-related protein 2]]

2ys3

From Proteopedia

Current revision

Solution structure of the PH domain of Kindlin-3 from human

Structural highlights

Disease

Function

Evolutionary Conservation

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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