7c3m: Difference between revisions

Latest revision as of 10:50, 27 March 2024

Structure of FERM protein

Structural highlights

7c3m is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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:https://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:https://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:https://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:https://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:https://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:https://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:https://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:https://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:https://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:https://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:https://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:https://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:https://dx.doi.org/10.1038/nm.1917

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1182/blood-2008-10-182154

[2] 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:https://dx.doi.org/10.1038/nm.1931

[3] 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:https://dx.doi.org/10.1038/nm.1917

[4] 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:https://dx.doi.org/10.1182/blood-2008-06-163162

[5] 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:https://dx.doi.org/10.1182/blood-2009-04-218636

[6] 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:https://dx.doi.org/10.1016/j.bbrc.2008.02.024

[7] 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:https://dx.doi.org/10.1182/blood-2008-10-182154

[8] 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:https://dx.doi.org/10.1038/nm.1931

[9] 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:https://dx.doi.org/10.1038/nm.1917

[10] 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:https://dx.doi.org/10.1016/j.bbrc.2008.02.024

[11] 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:https://dx.doi.org/10.1182/blood-2008-10-182154

[12] 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:https://dx.doi.org/10.1038/nm.1931

[13] 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:https://dx.doi.org/10.1038/nm.1917

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@@ Line 1: / Line 1: @@
-==structure of FERM protein==
+==Structure of FERM protein==
-<StructureSection load='7c3m' size='340' side='right'caption='[[7c3m]]' scene=''>
+<StructureSection load='7c3m' size='340' side='right'caption='[[7c3m]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C3M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7C3M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7c3m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C3M FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7c3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c3m OCA], [http://pdbe.org/7c3m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7c3m RCSB], [http://www.ebi.ac.uk/pdbsum/7c3m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7c3m ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#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=7c3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c3m OCA], [https://pdbe.org/7c3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c3m RCSB], [https://www.ebi.ac.uk/pdbsum/7c3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c3m ProSAT]</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>
+== 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>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Bu, W, Loh, ZY, Jin, S, Basu, S, Ero, R, Park, JE, Yan, X, Wang, M, Sze, SK, Tan, SM, Gao, YG]]
+[[Category: Basu S]]
+[[Category: Bu W]]
+[[Category: Ero R]]
+[[Category: Gao YG]]
+[[Category: Jin S]]
+[[Category: Loh ZY]]
+[[Category: Park JE]]
+[[Category: Sze SK]]
+[[Category: Tan SM]]
+[[Category: Wang M]]
+[[Category: Yan X]]

7c3m: Difference between revisions

Latest revision as of 10:50, 27 March 2024

Structure of FERM protein

Structural highlights

Disease

Function

References

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