Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 Jan 10;293(8):2815–2828. doi: 10.1074/jbc.RA117.000656

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2018 by The American Society for Biochemistry and Molecular Biology, Inc.

PMC Copyright notice

Figure 6. — Structural features of sAB-P1·MBP complex. A, sAB-P1 binds to the closed conformation of MBP interacting across the face of the binding pocket with the maltose trapped inside. B, superposition of MBP bound to sAB-P1 (green) with that of sAB-11M (slate) shows that sAB-P1 binds to the peristeric site of MBP in the closed form opposite to sAB-11M. C, interactions of the HC (magenta) and LC (blue) CDRs of sAB-P1 with the two helices (64–73 and 334–352) of MBP (green) at the peristeric interface. D, the relative orientations of the helices comprising residues 64–73 and 341–350 are different in open (salmon) and closed (green) forms of MBP. These helices in the closed conformation interact extensively with sAB-P1 (C), thereby imparting conformational specificity.