1lv9
From Proteopedia
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[[Image:1lv9.jpg|left|200px]] | [[Image:1lv9.jpg|left|200px]] | ||
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| - | + | {{STRUCTURE_1lv9| PDB=1lv9 | SCENE= }} | |
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'''CXCR3 Binding Chemokine IP-10/CXCL10''' | '''CXCR3 Binding Chemokine IP-10/CXCL10''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LV9 is a [[Single protein]] structure | + | 1LV9 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LV9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Keizer, D W.]] | [[Category: Keizer, D W.]] | ||
[[Category: Sykes, B D.]] | [[Category: Sykes, B D.]] | ||
| - | [[Category: | + | [[Category: Chemokine]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:19:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:19, 2 May 2008
CXCR3 Binding Chemokine IP-10/CXCL10
Overview
The structure of IP-10 was solved by NMR spectroscopy and represents the first structure from the class of agonists toward the receptor CXCR3. CXCR3 binding chemokines are unique in their ability to bind receptors from both the CC and CXC classes of chemokine receptors. An unusual structural feature of IP-10 was identified that may provide the basis for the ability of IP-10 to bind both CXCR3 and CCR3. The surface of IP-10 that interacts with the N-terminus of CXCR3 was defined by monitoring changes in the NMR spectrum of IP-10 upon addition of a CXCR3 N-terminal peptide. These studies indicated that the interaction involves a hydrophobic cleft, formed by the N-loop and 40s-loop region of IP-10, similar to the interaction surface observed for other chemokines such as IL-8. An additional region of interaction was observed that consists of a hydrophobic cleft formed by the N-terminus of IP-10 and 30s-loop of IP-10.
About this Structure
1LV9 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor interactions., Booth V, Keizer DW, Kamphuis MB, Clark-Lewis I, Sykes BD, Biochemistry. 2002 Aug 20;41(33):10418-25. PMID:12173928 Page seeded by OCA on Sat May 3 00:19:46 2008
