1qsv
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1qsv.gif|left|200px]] | + | [[Image:1qsv.gif|left|200px]] |
- | + | ||
- | '''THE VEGF-BINDING DOMAIN OF FLT-1, 20 NMR STRUCTURES''' | + | {{Structure |
+ | |PDB= 1qsv |SIZE=350|CAPTION= <scene name='initialview01'>1qsv</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''THE VEGF-BINDING DOMAIN OF FLT-1, 20 NMR STRUCTURES''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
- | 1QSV is a [ | + | 1QSV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSV OCA]. |
==Reference== | ==Reference== | ||
- | Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states., Starovasnik MA, Christinger HW, Wiesmann C, Champe MA, de Vos AM, Skelton NJ, J Mol Biol. 1999 Oct 29;293(3):531-44. PMID:[http:// | + | Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states., Starovasnik MA, Christinger HW, Wiesmann C, Champe MA, de Vos AM, Skelton NJ, J Mol Biol. 1999 Oct 29;293(3):531-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10543948 10543948] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 26: | Line 35: | ||
[[Category: vegf receptor]] | [[Category: vegf receptor]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:42:17 2008'' |
Revision as of 11:42, 20 March 2008
| |||||||
Coordinates: | save as pdb, mmCIF, xml |
THE VEGF-BINDING DOMAIN OF FLT-1, 20 NMR STRUCTURES
Contents |
Overview
The extracellular portion of the VEGF and PlGF receptor, Flt-1 (or VEGFR-1), consists of seven immunoglobulin-like domains. The second domain from the N terminus (Flt-1D2) is necessary and sufficient for high affinity VEGF binding. The 1.7 A resolution crystal structure of Flt-1D2 bound to VEGF revealed that this domain is a member of the I-set of the immunoglobulin superfamily, but has several unusual features including a region near the N terminus that bulges away from the domain rather than pairing with the neighboring beta-strand. Some of the residues in this region make contact with VEGF, raising the possibility that this bulge could be a consequence of VEGF binding and might not be present in the absence of ligand. Here we report the three-dimensional structure of Flt-1D2 in its uncomplexed form determined by NMR spectroscopy. A semi-automated method for NOE assignment that takes advantage of the previously solved crystal structure was used to facilitate rapid analysis of the 3D NOESY spectra. The solution structure is very similar to the previously reported VEGF-bound crystal structure; the N-terminal bulge is present, albeit in a different conformation. We also report the 2.7 A crystal structure of Flt-1D2 in complex with VEGF solved in a different crystal form that reveals yet another conformation for the N-terminal bulge region. (1)H-(15)N heteronuclear NOEs indicate this region is flexible in solution; the crystal structures show that this region is able to adopt more than one conformation even when bound to VEGF. Thus, VEGF-binding is not accompanied by significant structural change in Flt-1D2, and the unusual structural features of Flt-1D2 are an intrinsic property of this domain.
Disease
Known diseases associated with this structure: Fanconi renotubular syndrome OMIM:[134600], Jackson-Weiss syndrome OMIM:[136350], Kallmann syndrome 2 OMIM:[136350], Pfeiffer syndrome OMIM:[136350]
About this Structure
1QSV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states., Starovasnik MA, Christinger HW, Wiesmann C, Champe MA, de Vos AM, Skelton NJ, J Mol Biol. 1999 Oct 29;293(3):531-44. PMID:10543948
Page seeded by OCA on Thu Mar 20 13:42:17 2008