2qqm: Difference between revisions

Revision as of 19:41, 21 February 2008

Crystal Structure of the a2b1b2 Domains from Human Neuropilin-1

OverviewOverview

Neuropilins (Nrps) are co-receptors for class 3 semaphorins and vascular endothelial growth factors and important for the development of the nervous system and the vasculature. The extracellular portion of Nrp is composed of two domains that are essential for semaphorin binding (a1a2), two domains necessary for VEGF binding (b1b2), and one domain critical for receptor dimerization (c). We report several crystal structures of Nrp1 and Nrp2 fragments alone and in complex with antibodies that selectively block either semaphorin or vascular endothelial growth factor (VEGF) binding. In these structures, Nrps adopt an unexpected domain arrangement in which the a2, b1, and b2 domains form a tightly packed core that is only loosely connected to the a1 domain. The locations of the antibody epitopes together with in vitro experiments indicate that VEGF and semaphorin do not directly compete for Nrp binding. Based upon our structural and functional data, we propose possible models for ligand binding to neuropilins.

About this StructureAbout this Structure

2QQM is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding., Appleton BA, Wu P, Maloney J, Yin J, Liang WC, Stawicki S, Mortara K, Bowman KK, Elliott JM, Desmarais W, Bazan JF, Bagri A, Tessier-Lavigne M, Koch AW, Wu Y, Watts RJ, Wiesmann C, EMBO J. 2007 Nov 28;26(23):4902-12. Epub 2007 Nov 8. PMID:17989695

Page seeded by OCA on Thu Feb 21 18:41:26 2008

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 ==Overview==
-Neuropilins (Nrps) are co-receptors for class 3 semaphorins and vascular, endothelial growth factors and important for the development of the, nervous system and the vasculature. The extracellular portion of Nrp is, composed of two domains that are essential for semaphorin binding (a1a2), two domains necessary for VEGF binding (b1b2), and one domain critical for, receptor dimerization (c). We report several crystal structures of Nrp1, and Nrp2 fragments alone and in complex with antibodies that selectively, block either semaphorin or vascular endothelial growth factor (VEGF), binding. In these structures, Nrps adopt an unexpected domain arrangement, in which the a2, b1, and b2 domains form a tightly packed core that is, only loosely connected to the a1 domain. The locations of the antibody, epitopes together with in vitro experiments indicate that VEGF and, semaphorin do not directly compete for Nrp binding. Based upon our, structural and functional data, we propose possible models for ligand, binding to neuropilins.
+Neuropilins (Nrps) are co-receptors for class 3 semaphorins and vascular endothelial growth factors and important for the development of the nervous system and the vasculature. The extracellular portion of Nrp is composed of two domains that are essential for semaphorin binding (a1a2), two domains necessary for VEGF binding (b1b2), and one domain critical for receptor dimerization (c). We report several crystal structures of Nrp1 and Nrp2 fragments alone and in complex with antibodies that selectively block either semaphorin or vascular endothelial growth factor (VEGF) binding. In these structures, Nrps adopt an unexpected domain arrangement in which the a2, b1, and b2 domains form a tightly packed core that is only loosely connected to the a1 domain. The locations of the antibody epitopes together with in vitro experiments indicate that VEGF and semaphorin do not directly compete for Nrp binding. Based upon our structural and functional data, we propose possible models for ligand binding to neuropilins.
 ==About this Structure==
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 ==Reference==
-Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding., Appleton BA, Wu P, Maloney J, Yin J, Liang WC, Stawicki S, Mortara K, Bowman KK, Elliott JM, Desmarais W, Bazan JF, Bagri A, Tessier-Lavigne M, Koch AW, Wu Y, Watts RJ, Wiesmann C, EMBO J. 2007 Nov 8;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17989695 17989695]
+Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding., Appleton BA, Wu P, Maloney J, Yin J, Liang WC, Stawicki S, Mortara K, Bowman KK, Elliott JM, Desmarais W, Bazan JF, Bagri A, Tessier-Lavigne M, Koch AW, Wu Y, Watts RJ, Wiesmann C, EMBO J. 2007 Nov 28;26(23):4902-12. Epub 2007 Nov 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17989695 17989695]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Appleton, B.A.]]
+[[Category: Appleton, B A.]]
 [[Category: Wiesmann, C.]]
 [[Category: CA]]
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 [[Category: vegf receptor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:03:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:26 2008''