1v4l
From Proteopedia
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'''Crystal structure of a platelet agglutination factor isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus)''' | '''Crystal structure of a platelet agglutination factor isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus)''' | ||
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[[Category: Ko, T P.]] | [[Category: Ko, T P.]] | ||
[[Category: Wang, A H.J.]] | [[Category: Wang, A H.J.]] | ||
| - | [[Category: | + | [[Category: Lectin-like]] |
| - | [[Category: | + | [[Category: Square-shaped ring]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:04:21 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:04, 3 May 2008
Crystal structure of a platelet agglutination factor isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus)
Overview
Platelet glycoprotein Ib (GPIb)-binding proteins (GPIb-BPs) from snake venoms are usually C-type lectins, which target specific sites of GPIbalpha and elicit distinct effects on platelets. In the present paper, we report a tetrameric platelet-agglutinating factor (molecular mass 121.1 kDa), termed mucrocetin, purified from the venom of Taiwan habu (Trimeresurus mucrosquamatus ). Mucrocetin is a GPIbalpha agonist with a binding site distinct from that of flavocetin-A (a snake venom GPIbalpha antagonist) on GPIbalpha, in spite of the high sequence identity (94.6%) between the two venom lectins. The crystal structure of mucrocetin was solved and refined to 2.8 A (1 A=0.1 nm) resolution, which shows an interesting crystal packing of six-layer cylinders of doughnut-shaped molecules. The four alphabeta heterodimers are arranged in an unusual square-shaped ring stabilized by four interdimer 'head-to-tail' disulphide bridges. Detailed structural comparison between mucrocetin and flavocetin-A suggests that their disparate platelet effects are probably attributable to different charge distributions on the putative concave binding surface. A unique positively charged patch on the binding surface of mucrocetin, formed by Lys102, Lys108, Lys109 and Arg123 in the alpha-subunit coupled with Lys22, Lys102, Lys116 and Arg117 in the beta-subunit, appears to be the primary determinant of its platelet-agglutinating activity. Conceivably, this interesting venom factor may provide a useful tool to study platelet agglutination by binding to the GPIb-IX-V complex.
About this Structure
1V4L is a Protein complex structure of sequences from Protobothrops mucrosquamatus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a platelet-agglutinating factor isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus)., Huang KF, Ko TP, Hung CC, Chu J, Wang AH, Chiou SH, Biochem J. 2004 Mar 1;378(Pt 2):399-407. PMID:14613481 Page seeded by OCA on Sat May 3 12:04:21 2008
